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phsA

Gene
phsA
Protein
Thiosulfate reductase molybdopterin-containing subunit PhsA
Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Length
758 amino acids
Function
Component of the PhsABC thiosulfate reductase that catalyzes the reduction of thiosulfate to sulfite and hydrogen sulfide, with menaquinol as the sole electron donor. Proton motive force (PMF) is required to drive transmembrane electron transfer within the reductase. The PhsA subunit contains the active site molybdenum-bis(molybdopterin guanine dinucleotide) (Mo-bis-MGD) cofactor.
Similarity
Belongs to the prokaryotic molybdopterin-containing oxidoreductase family.
Mass
82.8 kDa
Sequence
MSISRRSFLQGVGIGCSACALGAFPPGALARNPIAGINGKTTLTPSLCEMCSFRCPIQAQVVNNKTVFIQGNPSAPQQGTRICARGGSGVSLVNDPQRIVKPMKRTGPRGDGEWQVISWQQAYQEIAAKMNAIKAQHGPESVAFSSKSGSLSSHLFHLATAFGSPNTFTHASTCPAGKAIAAKVMMGGDLAMDIANTRYLVSFGHNLYEGIEVADTHELMTAQEKGAKMVSFDPRLSIFSSKADEWHAIRPGGDLAVLLAMCHVMIDEQLYDASFVERYTSGFEQLAQAVKETTPEWAAAQADVPADVIVRVTRELAACAPHAIVSPGHRATFSQEEIDMRRMIFTLNVLLGNIEREGGLYQKKNASVYNKLAGEKVAPTLAKLNIKNMPKPTAQRIDLVAPQFKYIAAGGGVVQSIIDSALTQKPYPIKAWIMSRHNPFQTVTCRSDLVKTVEQLDLVVSCDVYLSESAAYADYLLPECTYLERDEEVSDMSGLHPAYALRQQVVEPIGEARPSWQIWKELGEQLGLGQYYPWQDMQTRQLYQLNGDHALAKELRQKGYLEWGVPLLLREPESVRQFTARYPGAIATDSDNTYGEQLRFKSPSGKIELYSATLEELLPGYGVPRVRDFALKKENELYFIQGKVAVHTNGATQYVPLLSELMWDNAVWVHPQTAQEKGIKTGDEIWLENATGKEKGKALVTPGIRPDTLFVYMGFGAKAGAKTAATTHGIHCGNLLPHVTSPVSGTVVHTAGVTLSRA

Gene
phsA
Protein
O-aminophenol oxidase
Organism
Streptomyces antibioticus
Length
643 amino acids
Function
Could be involved in the spore pigmentation and melanin production. Catalyzes the oxidative coupling of 2-aminophenols to form the 2-aminophenoxazinone chromophore. 2-aminophenoxazinone synthesis proceeds via a sequence of three consecutive 2-electron aminophenol oxidations. First, the o-aminophenol is oxidized by two electrons to the quinone imine, which then conjugates to a second o-aminophenol molecule while still bound to the enzyme. This product is further oxidized by two electrons to give rise to the p-quinone imine. The last two steps of the reaction, another conjugation to generate the tricyclic structure and a final two-electron oxidation to yield the 2-aminophenoxazinone product, are thought to be non-enzymatic. It can also uuse 3-hydroxyanthranilic acid (HAA), 4-methyl-3-hydroxyanthranilic acid (MHA), 3,4-dihydroxy-L-phenylalanine (L-DOPA), ferrocyanide and thiophenol as substrates.
Similarity
Belongs to the multicopper oxidase family.
Mass
70.245 kDa
Sequence
MTDMIEQSDDRIDPIDGVLADGVLADDVLAKEREQAPAPGELTPFAAPLTVPPVLRPASDEVTRETEIALRPTWVRLHPQLPPTLMWGYDGQVPGPTIEVRRGQRVRIAWTNRIPKGSEYPVTSVEVPLGPPGTPAPNTEPGRGGVEPNKDVAALPAWSVTHLHGAQTGGGNDGWADNAVGFGDAQLSEYPNDHQATQWWYHDHAMNITRWNVMAGLYGTYLVRDDEEDALGLPSGDREIPLLIADRNLDTDEDGRLNGRLLHKTVIVQQSNPETGKPVSIPFFGPYTTVNGRIWPYADVDDGWYRLRLVNASNARIYNLVLIDEDDRPVPGVVHQIGSDGGLLPRPVPVDFDDTLPVLSAAPAERFDLLVDFRALGGRRLRLVDKGPGAPAGTPDPLGGVRYPEVMEFRVRETCEEDSFALPEVLSGSFRRMSHDIPHGHRLIVLTPPGTKGSGGHPEIWEMAEVEDPADVQVPAEGVIQVTGADGRTKTYRRTAATFNDGLGFTIGEGTHEQWTFLNLSPILHPMHIHLADFQVLGRDAYDASGFDLALGGTRTPVRLDPDTPVPLAPNELGHKDVFQVPGPQGLRVMGKFDGAYGRFMYHCHLLEHEDMGMMRPFVVMPPEALKFDHGGAHGGHGEGHTG