ID A3JTW1_9RHOB Unreviewed; 921 AA.
AC A3JTW1;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 90.
DE SubName: Full=Formate dehydrogenase, alpha subunit {ECO:0000313|EMBL:EBA02961.1};
GN ORFNames=RB2150_03314 {ECO:0000313|EMBL:EBA02961.1};
OS Rhodobacteraceae bacterium HTCC2150.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae.
OX NCBI_TaxID=388401 {ECO:0000313|EMBL:EBA02961.1, ECO:0000313|Proteomes:UP000004731};
RN [1] {ECO:0000313|EMBL:EBA02961.1, ECO:0000313|Proteomes:UP000004731}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTCC2150 {ECO:0000313|EMBL:EBA02961.1,
RC ECO:0000313|Proteomes:UP000004731};
RX PubMed=20889754; DOI=10.1128/JB.01088-10;
RA Kang I., Oh H.M., Vergin K.L., Giovannoni S.J., Cho J.C.;
RT "Genome sequence of the marine alphaproteobacterium HTCC2150, assigned to
RT the Roseobacter clade.";
RL J. Bacteriol. 192:6315-6316(2010).
CC -!- COFACTOR:
CC Name=Mo-bis(molybdopterin guanine dinucleotide);
CC Xref=ChEBI:CHEBI:60539; Evidence={ECO:0000256|ARBA:ARBA00001942};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- SIMILARITY: In the C-terminal section; belongs to the prokaryotic
CC molybdopterin-containing oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00007023}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EBA02961.1}.
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DR EMBL; AAXZ01000005; EBA02961.1; -; Genomic_DNA.
DR AlphaFoldDB; A3JTW1; -.
DR eggNOG; COG3383; Bacteria.
DR OrthoDB; 9816402at2; -.
DR Proteomes; UP000004731; Unassembled WGS sequence.
DR GO; GO:1990204; C:oxidoreductase complex; IEA:UniProt.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0008863; F:formate dehydrogenase (NAD+) activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR GO; GO:0045333; P:cellular respiration; IEA:UniProt.
DR GO; GO:0015942; P:formate metabolic process; IEA:InterPro.
DR CDD; cd00207; fer2; 1.
DR CDD; cd02790; MopB_CT_Formate-Dh_H; 1.
DR CDD; cd02753; MopB_Formate-Dh-H; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.10.20.740; -; 1.
DR Gene3D; 3.30.70.20; -; 1.
DR Gene3D; 3.40.50.740; -; 1.
DR Gene3D; 2.20.25.90; ADC-like domains; 1.
DR Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 1.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR041925; CT_Formate-Dh_H.
DR InterPro; IPR041924; Formate_Dh-H_N.
DR InterPro; IPR006478; Formate_DH_asu.
DR InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR NCBIfam; TIGR01591; Fdh-alpha; 1.
DR PANTHER; PTHR43105:SF15; FORMATE DEHYDROGENASE H; 1.
DR PANTHER; PTHR43105; RESPIRATORY NITRATE REDUCTASE; 1.
DR Pfam; PF13510; Fer2_4; 1.
DR Pfam; PF12838; Fer4_7; 1.
DR Pfam; PF04879; Molybdop_Fe4S4; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR PIRSF; PIRSF036643; FDH_alpha; 1.
DR SMART; SM00926; Molybdop_Fe4S4; 1.
DR SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR SUPFAM; SSF50692; ADC-like; 1.
DR SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
PE 3: Inferred from homology;
KW 2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
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:UP000004731}.
FT DOMAIN 3..83
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 142..172
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 185..214
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 227..282
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 921 AA; 100938 MW; DBBBBD6325D8BA50 CRC64;
MTDTVTFNLN GEDVTVERGL TVWEAANGRG LKIPHLCHKD ATAYVPDGNC RACMVEVEGE
RTLVASCIRP AADGMVVKTD SARAEKARKM VMELLVTDQP DRDAAHDKSS HLWDMADMQD
VSDSRFPKLE ETRVPLLDAS HLAMSVNLDA CIQCNLCVRA CRDVQVNDVI GLSGRGADAK
ITFDFDDPMG ASSCVACGEC VQACPTGALM PATVVDEALV GDSKAFDREV ESVCPYCGVG
CQLSFKIKDE KIAWVEGIEG PANENRLCVK GRFGFDYIAH PHRLTKPLIR RDDAPAKGLN
VDPGNLSTHF REASWEEAFE FAGRGMKGRG REIAGFGSAK CSNEEAYLFQ KLIREAFKHN
NVDHCTRLCH ASSVSALLEN VGSGAVTATF NEIENADVAI VIGCNPSENH PVAATYFKQF
AKRGGKLIII DPRGTAMKRH AEHMLQFRPG TDVALLNAIM NVIVEEKLYD QNYIDTMTEN
WDEMKAHLAD FTPEAMSPLC GISPEEIRQV ARTYANADAA MIFWGMGISQ HIHGTDNSRC
LISLALMTGQ TGRPGAGLHP LRGQNNVQGA SDAGLIPMFL PDYQSVEDDG VRSAFTDVWG
TDDFSSQKGL TVVEIMDAIH DDKIKGMYIL GENPAMSDPD VEHARDALAK LDCLVVQDIF
LTETANYADV IFPSSAWPEK TGTVTNTNRQ VQMGRPAVSP PGDAREDWWI TVQLANHLGL
DWNYTHPKEV FAEMKLNMGS LDNITWDRLE TTAVTYPSLT PDDPGQPIVF GDKFPRPSGR
ARFTPANVTA PAEVPDADFP MILTTGRQLE HWHTGSMTRR ATVLDWAEPE ANASLHPKTL
RAMGVKAGEM ITLETRRGKI NIMARVDRAV AEDMVFLPFA YVEAAANILT NPKLDPFGKI
PEFKFSACRA RAADPVTEAA E
//
