dsrA

Sulfite reductase, dissimilatory-type subunit alpha

418 amino acids

Catalyzes the reduction of sulfite to sulfide. This is the terminal oxidation reaction in sulfate respiration.

47.525 kDa

MSETPLLDELEKGPWPSFVKEIKKTAELMEKAAAEGKDVKMPKGARGLLKQLEISYKDKKTHWKHGGIVSVVGYGGGVIGRYSDLGEQIPEVEHFHTMRINQPSGWFYSTKALRGLCDVWEKWGSGLTNFHGSTGDIIFLGTRSEYLQPCFEDLGNLEIPFDIGGSGSDLRTPSACMGPALCEFACYDTLELCYDLTMTYQDELHRPMWPYKFKIKCAGCPNDCVASKARSDFAIIGTWKDDIKVDQEAVKEYASWMDIENEVVKLCPTGAIKWDGKELTIDNRECVRCMHCINKMPKALKPGDERGATILIGGKAPFVEGAVIGWVAVPFVEVEKPYDEIKEILEAIWDWWDEEGKFRERIGELIWRKGMREFLKVIGREADVRMVKAPRNNPFMFFEKDELKPSAYTEELKKRGMW

dsrA

Sulfite reductase, dissimilatory-type subunit alpha

417 amino acids

Catalyzes the reduction of sulfite to sulfide. This is the terminal oxidation reaction in sulfate respiration.

46.791 kDa

MAIDKHATPMLDQLETGPWPSFISGIKRLRDQHPDARINAVTNDLLGQLEHSYETRKGYWKGGTVSVFGYGGGIIPRFSEVGKVFPSSKEFHTVRVQPPAGNHYTTAMLRQLADTWEKYGSGLITFHGQTGNIMFIGVDTPNTQNFFDEINDYGWDLGGAGPCVRTAMSCVGSARCEMSCTNELKAHRLLVNNFTDDVHRPALPYKFKFKVSGCPNDCQNAIERSDFAVLGTWRDDMKVDQAEVKHYIADKGRQYYIDNVITRCPTKALSLNDDDTLDVNNRDCVRCMHCLNVMPKALHPGDDKGVTILIGGKRTLKIGDLMGTVVVPFKKLETEEDYESLVELAETIIDFWAENGLEHERCGEMIERIGLANFLEGIGIEPDPNMLSHPRQSSYIRMDGWDEAAEEWFARQAEAGR

dsrA

Sulfite reductase, dissimilatory-type subunit alpha

198 amino acids

Part of the complex that catalyzes the reduction of sulfite to sulfide. The alpha and beta subunits may have arisen by gene duplication. They both bind 2 iron-sulfur clusters, but the alpha subunit seems to be catalytically inactive, due to substitutions along the putative substrate access channel, and because it binds sirohydrochlorin (the dematallated form of siroheme) instead of siroheme.

22.384 kDa

single

WKDDIKIDQEAVKAYVGGEFKPNAGAHAGRDWGKFDIEAEVVGLCPTGCMTYESGTLSIDNKNCTRCMHCINTMPRALKIGDERGASILVGAKAPVLDGAQMGSLLIPFIAAEEPFDEVKEVIENIWEWWMEEGKNRERLGETMKRVGFQKLLEVTGTKAVPQHVSEPRHNPYIFFKEEEVPGGWSRDISDYRKRHMR

dsrA

Sulfite reductase, dissimilatory-type subunit alpha

198 amino acids

Part of the complex that catalyzes the reduction of sulfite to sulfide. The alpha and beta subunits may have arisen by gene duplication. They both bind 2 iron-sulfur clusters, but the alpha subunit seems to be catalytically inactive, due to substitutions along the putative substrate access channel, and because it binds sirohydrochlorin (the dematallated form of siroheme) instead of siroheme.

22.384 kDa

single

WKDDIKIDQEAVKAYVGGEFKPNAGAHAGRDWGKFDIEAEVVGLCPTGCMTYESGTLSIDNKNCTRCMHCINTMPRALKIGDERGASILVGAKAPVLDGAQMGSLLIPFIAAEEPFDEVKEVIENIWEWWMEEGKNRERLGETMKRVGFQKLLEVTGTKAVPQHVSEPRHNPYIFFKEEEVPGGWSRDISDYRKRHMR