About Products Protein Database Contact

hemW

Gene
hemW
Protein
Heme chaperone HemW
Organism
Synechocystis sp. (strain PCC 6803 / Kazusa)
Length
412 amino acids
Function
Probably acts as a heme chaperone, transferring heme to an unknown acceptor. Binds one molecule of heme per monomer, possibly covalently (By similarity). Binds 1 [2Fe-2S] cluster. Although this protein has sequence motifs typically found in proteins binding the [4Fe-4S]-AdoMet radical-SAM cluster and S-adenosylmethionine, spectroscopic evidence suggests that a [2Fe-2S] cluster is present; S-adenosylmethionine was not detected. Has no detectable coproporphyrinogen-III oxidase activity (PubMed:20194361).
Similarity
Belongs to the anaerobic coproporphyrinogen-III oxidase family. HemW subfamily.
Mass
46.447 kDa
Sequence
MNTGTYLMPTAAYIHIPFCRQRCFYCDFPIAVTGFQSLTLDGWVGEYVEAVCREIAGQQHQGQPLQTVFFGGGTPSLLPITGLEKILLAVDQYLGIAPDAEISIEIDPGTFDQVQLQGYKNLGINRFSLGVQAFQDNLLALCGRHHRRRDIDQALTAIAKENIENWSLDLITGLPEQTAADWHSSLTLALAAGPKHISCYDLVLEPQTVFDKWEQRGKLAVPPPERSADFYRHGQEVLTQAGFHHYEISNYGRPGHQCRHNQIYWRNLPYYGLGMGATSYIDGKRFGRPRTRNGYYQWLESWLNQGCPIPGERVSPLENLLESLMLGLRLTAGVTWAQLPSVNQTEKAKILATLTSFGDRRWLEFYGEDNQMLAPNQTTTETVQRFCFTDPEGILYSNQILSALFAALEEDF

Gene
hemW
Protein
Heme chaperone HemW
Organism
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Length
383 amino acids
Function
Probably acts as a heme chaperone, transferring heme to an unknown acceptor. Binds one molecule of heme per monomer, possibly covalently (By similarity). Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine (By similarity).
Similarity
Belongs to the anaerobic coproporphyrinogen-III oxidase family. HemW subfamily.
Mass
44.105 kDa
Sequence
MPKLPPLSLYIHIPWCVQKCPYCDFNSHAQKSDIPEQDYIYHLLQDLQADLQRFKDSIQQRKLHSIFIGGGTPSLFSAESIAYLLKEIKKQIDFEDNIEITLEANPGTVEAERFKGYVSAGIMRISMGIQSFNDDKLQRLGRIHNAAEAKSAVNLAKVSGLKSFNLDLMHGLPNQTLEEALDDLRQAIELSPPHISWYQLTIEPNTMFAYRPPKLPDDDALWDIFEQGHQLLTMAGYQQYETSAYAKAGFQCKHNLNYWRFGDYLAIGCGAHGKLTFPTGEITRFSKTKHPKGYLRGEYLYEEKNVPKIDRPFEFFMNRFRLLEAVPKQEFEDYTGLSQSAVKNQIDFAIQQNYIVENADSWQITEHGKLFLNELLELFLTEE

Gene
hemW
Protein
Heme chaperone HemW
Organism
Bacillus subtilis (strain 168)
Length
379 amino acids
Function
Probably acts as a heme chaperone, transferring heme to an unknown acceptor. Binds one molecule of heme per monomer, possibly covalently (By similarity). Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine (By similarity).
Similarity
Belongs to the anaerobic coproporphyrinogen-III oxidase family. HemW subfamily.
Mass
42.888 kDa
Sequence
MKSAYIHIPFCEHICHYCDFNKYFIQSQPVDEYLNALEQEMINTIAKTGQPDLKTIFIGGGTPTSLSEEQLKKLMDMINRVLKPSSDLSEFAVEANPDDLSAEKLKILKEAGVNRLSFGVQTFEDDLLEKIGRVHKQKDVFTSFERAREIGFENISLDLMFGLPGQTLKHLEHSINTALSLDAEHYSVYSLIVEPKTVFYNLMQKGRLHLPPQEQEAEMYEIVMSKMEAHGIHQYEISNFAKAGMESKHNLTYWSNEQYFGFGAGAHGYIGGTRTVNVGPVKHYIDLIAEKGFPYRDTHEVTTEEQIEEEMFLGLRKTAGVSKKRFAEKYGRSLDGLFPSVLKDLAEKGLIHNSESAVYLTHQGKLLGNEVFGAFLGEL

Gene
hemW
Protein
Heme chaperone HemW
Organism
Lactococcus lactis subsp. lactis (strain IL1403)
Length
379 amino acids
Function
Could serve in the delivery of heme to a membrane-localized target protein (Probable). Binds one molecule of heme per monomer, possibly covalently; heme and Fe-S cluster binding are independent. Incubation with the reductant sodium dithionite increases binding. Does not have coproporphyrinogen III dehydrogenase activity in vitro, does not complement an E.coli hemN deletion in vivo (PubMed:22142238). Binds 1 Fe-S cluster, it is probably [4Fe-4S]. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine; only dimeric protein has the cluster (Probable).
Similarity
Belongs to the anaerobic coproporphyrinogen-III oxidase family. HemW subfamily.
Mass
43.553 kDa
Sequence
MLQKPNSAYFHIPFCSHICYYCDFAKVLMTGQPIDAYIESLIEEFQSFEIEKLRTIYIGGGTPSVLSAQQLERLLTAIAEQLDLEVLEEFTVEANPGDLSDEVIKVLADSAVNRISLGVQTFNNALLKKIGRTHTEVQVYDSVERLKKAGFENITIDLIYALPGQTMEMVKSDVEKFLELKLPHVALYSLILEDHTVFMNRQRRGLLRLPSEDKNADMYEYIMDILAKNGYNHYEVSNFGLPGFESKHNITYWDNEEYYGIGAGASGYLAGIRYKNLGPVHHYLKAAPTEKRINEEVLSKKSQIEEEMFLGLRKKSGVLVEKFENKFKCSFEKLYGEQITELINQKLLYNDRQRIHMTDKGFELGNNVFEKFLLDDINF

Gene
hemW
Protein
Heme chaperone HemW
Organism
Escherichia coli (strain K12)
Length
378 amino acids
Function
Probably acts as a heme chaperone, transferring heme to the NarI subunit of the respiratory enzyme nitrate reductase; transfer may be stimulated by NADH. Binds one molecule of heme per monomer, possibly covalently. Heme binding is not affected by either [4Fe-4S] or S-adenosyl-L-methionine (SAM)-binding. Does not have coproporphyrinogen III dehydrogenase activity in vitro (PubMed:29282292). Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine (Probable).
Similarity
Belongs to the anaerobic coproporphyrinogen-III oxidase family. HemW subfamily.
Mass
42.584 kDa
Sequence
MVKLPPLSLYIHIPWCVQKCPYCDFNSHALKGEVPHDDYVQHLLNDLDNDVAYAQGREVKTIFIGGGTPSLLSGPAMQTLLDGVRARLPLAADAEITMEANPGTVEADRFVDYQRAGVNRISIGVQSFSEEKLKRLGRIHGPQEAKRAAKLASGLGLRSFNLDLMHGLPDQSLEEALGDLRQAIELNPPHLSWYQLTIEPNTLFGSRPPVLPDDDALWDIFEQGHQLLTAAGYQQYETSAYAKPGYQCQHNLNYWRFGDYIGIGCGAHGKVTFPDGRILRTTKTRHPRGFMQGRYLESQRDVEATDKPFEFFMNRFRLLEAAPRVEFIAYTGLCEDVIRPQLDEAIAQGYLTECADYWQITEHGKLFLNSLLELFLAE

Gene
hemW
Protein
Heme chaperone HemW
Organism
Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS)
Length
376 amino acids
Function
Probably acts as a heme chaperone, transferring heme to an unknown acceptor. Binds one molecule of heme per monomer, possibly covalently (By similarity). Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine (By similarity).
Similarity
Belongs to the anaerobic coproporphyrinogen-III oxidase family. HemW subfamily.
Mass
43.905 kDa
Sequence
MFTLPPISLYIHIPWCLKKCGYCDFYSYVSKEIIPENKYIEHLLRDFERDLSLINNRNINTIFIGGGTPSLLKNTSIKNLLNGIKKRKIISKNIEISIEANPKTLEYQNFIQYKNSGINRFSLGIQTFNSKMLKKIERTYNSKDAMNAIIESKKISDNINLDLMYGLPGQSLEEALSDLQIAIQCNPSHISWYQLTIEPNTVFYAKKIQTPHQDVVFNMLIEGDKLLKKAGYKKYEISSYSKFNYQCQHNLNYWNFGDYIGIGCGSHGKITQKNGEIIRTIKNKNINDFLSGKYINSVYQVSKRDKIFEYFMNVFRLYKPIFKKHFRENTNIEESFIEKNIQIAIQEGFLINQSDCWHTTKKGKNFLNSLLEIFLK

Gene
hemW
Protein
Heme chaperone HemW
Organism
Buchnera aphidicola subsp. Schizaphis graminum (strain Sg)
Length
376 amino acids
Function
Probably acts as a heme chaperone, transferring heme to an unknown acceptor. Binds one molecule of heme per monomer, possibly covalently (By similarity). Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine (By similarity).
Similarity
Belongs to the anaerobic coproporphyrinogen-III oxidase family. HemW subfamily.
Mass
44.581 kDa
Sequence
MFKLPPISLYIHIPWCIKKCGYCDFYSYVNKSFIPEKEYIDHLLKDLEKDLSLIKEREINSIFIGGGTPSLLKSSSIKKMMREIKKRINISNTAEITIEANPTTLEYKRFFNYKKSGINRFSIGVQTFNSDLLKKIERTYNKREAILAVEEIKKINKNFNLDIMYGLPNQSLKDVLLDLQYAVKYNPTHISWYQLTLEPNTPFYVKKLNLPNENNIFKMLVEGEKFLKQSGYKKYEISSYAKLNYECQHNLNYWNFGDYIGIGCSAHGKITQINGDIIRTIKNKNINDFMNGKYLKHKNFVLKKDKPFEYFMNIFRLYKPVLKRQFEERTNINQNYIKEKIKKAIEKGYLKNKIDFWDTTKKGKMFLNSLLKIFLD

Gene
hemW
Protein
Heme chaperone HemW
Organism
Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Length
375 amino acids
Function
Probably acts as a heme chaperone, transferring heme to an unknown acceptor. Binds one molecule of heme per monomer, possibly covalently (By similarity). Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine (By similarity).
Similarity
Belongs to the anaerobic coproporphyrinogen-III oxidase family. HemW subfamily.
Mass
40.334 kDa
Sequence
MPGQPFGVYLHVPFCLTRCGYCDFNTYTPAQLGGVSPDRWLLALRAELELAAAKLDAPTVHTVYVGGGTPSLLGGERLATLLDMVRDHFVLAPDAEVSTEANPESTWPEFFATIRAAGYTRVSLGMQSVAPRVLATLDRVHSPGRAAAAATEAIAEGFTHVNLDLIYGTPGESDDDLVRSVDAAVQAGVDHVSAYALVVEHGTALARRVRRGELAAPDDDVLAHRYELVDARLSAAGFAWYEVSNWCRPGGECRHNLGYWDGGQWWGAGPGAHGYIGVTRWWNVKHPNTYAEILAGATLPVAGFEQLGADALHTEDVLLKVRLRQGLPLARLGAAERERAEAVLADGLLDYHGDRLVLTGRGRLLADAVVRTLLG

Gene
hemW
Protein
Heme chaperone HemW
Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Length
375 amino acids
Function
Probably acts as a heme chaperone, transferring heme to an unknown acceptor. Binds one molecule of heme per monomer, possibly covalently (By similarity). Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine (By similarity).
Similarity
Belongs to the anaerobic coproporphyrinogen-III oxidase family. HemW subfamily.
Mass
40.334 kDa
Sequence
MPGQPFGVYLHVPFCLTRCGYCDFNTYTPAQLGGVSPDRWLLALRAELELAAAKLDAPTVHTVYVGGGTPSLLGGERLATLLDMVRDHFVLAPDAEVSTEANPESTWPEFFATIRAAGYTRVSLGMQSVAPRVLATLDRVHSPGRAAAAATEAIAEGFTHVNLDLIYGTPGESDDDLVRSVDAAVQAGVDHVSAYALVVEHGTALARRVRRGELAAPDDDVLAHRYELVDARLSAAGFAWYEVSNWCRPGGECRHNLGYWDGGQWWGAGPGAHGYIGVTRWWNVKHPNTYAEILAGATLPVAGFEQLGADALHTEDVLLKVRLRQGLPLARLGAAERERAEAVLADGLLDYHGDRLVLTGRGRLLADAVVRTLLG

Gene
hemW
Protein
Putative heme chaperone HemW-like protein
Organism
Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp)
Length
374 amino acids
Function
Might be a heme chaperone; in E.coli heme binds independently of binding to [4Fe-4S] or S-adenosyl-L-methionine.
Similarity
Belongs to the anaerobic coproporphyrinogen-III oxidase family. HemW subfamily.
Mass
44.752 kDa
Sequence
MKLLGLYINIPWPTKRYKYHDFKFPEYKKKINEKKYIHHLLQDLKKDSLLVPNRTINTIFIGGIAPNFFKLTSIKYLLKKIKNIIPISKNAENTIEFHISKLSEKKIFYYKKFGINRFSIRIQTFDQKKFNSLSKVHISKNILHKIKKINIEKFKNINLDLIYGLPKQSLQEALLDLKTAISLKPNHISWCEFYIEKNNNNYKNLSKSCNLNIIWKIFLQGEKLLKKSGYKKYEISSYSKTNYQCLHNLNYWKFGDYLGIGCNAHGKITQKNGKIIKTIKNKNLKKFMNGKYTYKNHIISKKNLSLEFFMNRLRLNTPIYRKDFKKYTYISEFYIKNEIKQAIEQNYLIETKKYWKMTSKGIQFLDSLLEIFIT