ID A0A1G5Q9H9_9GAMM Unreviewed; 914 AA.
AC A0A1G5Q9H9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Complex iron-sulfur molybdoenzyme family reductase subunit alpha {ECO:0000313|EMBL:SCZ58347.1};
GN ORFNames=SAMN03097708_01669 {ECO:0000313|EMBL:SCZ58347.1};
OS Thiohalomonas denitrificans.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC Ectothiorhodospiraceae; Thiohalomonas.
OX NCBI_TaxID=415747 {ECO:0000313|EMBL:SCZ58347.1, ECO:0000313|Proteomes:UP000199648};
RN [1] {ECO:0000313|EMBL:SCZ58347.1, ECO:0000313|Proteomes:UP000199648}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HLD2 {ECO:0000313|EMBL:SCZ58347.1,
RC ECO:0000313|Proteomes:UP000199648};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mo-bis(molybdopterin guanine dinucleotide);
CC Xref=ChEBI:CHEBI:60539; Evidence={ECO:0000256|ARBA:ARBA00001942};
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00010312}.
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DR EMBL; FMWD01000004; SCZ58347.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G5Q9H9; -.
DR STRING; 415747.SAMN03097708_01669; -.
DR OrthoDB; 9759518at2; -.
DR Proteomes; UP000199648; Unassembled WGS sequence.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR Gene3D; 3.40.50.12440; -; 4.
DR Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 1.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR PANTHER; PTHR43742:SF6; OXIDOREDUCTASE YYAE-RELATED; 1.
DR PANTHER; PTHR43742; TRIMETHYLAMINE-N-OXIDE REDUCTASE; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR SUPFAM; SSF50692; ADC-like; 1.
DR SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
PE 3: Inferred from homology;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000199648}.
FT DOMAIN 54..117
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 914 AA; 102419 MW; C57C41EB1E7B043B CRC64;
MDRREFLRNS TYCGLALAFG GPLTALRAHA TTAPGDQRWE GFYRDEFLDT RGDAQGFAFH
CSNCQGNCAW KVFAKDGRVT REEQSAAYPQ IHPRIPDANP RGCNKGIVHS REMYQGDRLL
HPLKRVGERG EGKWERVSWE EALEDIATRV VGTLTEQGPG ELMIYAGTGI LSQGRRAGPL
RLGSLLGAQR LYPASAVGDM FTGASLAYGL ANTGHSLDAW FDADAIFLWA INPIVTRIPD
AHYLNEARYN GATIYTISPD YNPSCKFATH WVPIKPGTDA YLAMSLLHVL LRDGHVDDAF
VREQTDLPFL VREDSGELLR HRDLRARGKE DVFYCWDEAS GKEQPMPGTP GHFKKTLRLG
KLRPALGGRY EVKGKEGELI PVTTVFERVR AEAANYPPDE TQAITGIHPE LVERMARDLA
RSDKAIINIG FALHKYVSGT MSCWAAALAC ALTGHAGERG GIDTEHNWSL NGIGPLSSPK
PARFASGFFS EWLNGDMQAS MDTHYSDEHL KATVGYDSKD VARQVAENRE SGKAYYGKPK
ALLLFADNMF RRNKTEAHHR EALLSNLDIF VDINHRMDST ALWADYVLPA KSHYESWDIR
GELGYHRFCN VTIPPEGLKP VGETRSEWTI CRGLSEAMAK VAKARGIEPI PDPDFLVEEG
DMAAPVMRDL QTLPDDFTDG GTLNNDEDVV RWLMENVEQI APWTPEDARK NGFVILNEKA
GFTSPLYANR PYHSFERNVY LREPYKTHSG RQQFFVDHPV FKEHGWTVPT AMGPLRPPSF
PLAFYTPHTR WGIHSQWRTN AQLLRLQRGE PYLWLNPATA AAREVGEDDR VRVFNDVGEF
IARVKLMPAV PPEAVVMDHA WEPHQFEKRI GLNSTVAGMI SLLELPDGWG HLTFSPNWDG
NMIAHESSVE VEKA
//