ID Q0FM40_SALBH Unreviewed; 973 AA.
AC Q0FM40;
DT 17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 17-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 94.
DE SubName: Full=NAD-dependent formate dehydrogenase, alpha subunit {ECO:0000313|EMBL:EAU45285.1};
GN ORFNames=R2601_17147 {ECO:0000313|EMBL:EAU45285.1};
OS Salipiger bermudensis (strain DSM 26914 / JCM 13377 / KCTC 12554 /
OS HTCC2601) (Pelagibaca bermudensis).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Salipiger.
OX NCBI_TaxID=314265 {ECO:0000313|EMBL:EAU45285.1, ECO:0000313|Proteomes:UP000006230};
RN [1] {ECO:0000313|EMBL:EAU45285.1, ECO:0000313|Proteomes:UP000006230}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 26914 / JCM 13377 / KCTC 12554 / HTCC2601
RC {ECO:0000313|Proteomes:UP000006230};
RX PubMed=20729358; DOI=10.1128/JB.00873-10;
RA Thrash J.C., Cho J.C., Ferriera S., Johnson J., Vergin K.L.,
RA Giovannoni S.J.;
RT "Genome sequences of Pelagibaca bermudensis HTCC2601T and Maritimibacter
RT alkaliphilus HTCC2654T, the type strains of two marine Roseobacter
RT genera.";
RL J. Bacteriol. 192:5552-5553(2010).
CC -!- COFACTOR:
CC Name=Mo-bis(molybdopterin guanine dinucleotide);
CC Xref=ChEBI:CHEBI:60539; Evidence={ECO:0000256|ARBA:ARBA00001942};
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000256|ARBA:ARBA00034078};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- SIMILARITY: Belongs to the complex I 75 kDa subunit family.
CC {ECO:0000256|ARBA:ARBA00005404}.
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:EAU45285.1}.
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DR EMBL; AATQ01000029; EAU45285.1; -; Genomic_DNA.
DR RefSeq; WP_007796970.1; NZ_DS022276.1.
DR AlphaFoldDB; Q0FM40; -.
DR STRING; 314265.R2601_17147; -.
DR eggNOG; COG3383; Bacteria.
DR HOGENOM; CLU_000422_4_1_5; -.
DR OrthoDB; 9816402at2; -.
DR Proteomes; UP000006230; 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; cd00508; MopB_CT_Fdh-Nap-like; 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; 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 InterPro; IPR019574; NADH_UbQ_OxRdtase_Gsu_4Fe4S-bd.
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 Pfam; PF10588; NADH-G_4Fe-4S_3; 1.
DR PIRSF; PIRSF036643; FDH_alpha; 1.
DR SMART; SM00926; Molybdop_Fe4S4; 1.
DR SMART; SM00929; NADH-G_4Fe-4S_3; 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; PS51839; 4FE4S_HC3; 1.
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:UP000006230}.
FT DOMAIN 21..99
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 99..138
FT /note="4Fe-4S His(Cys)3-ligated-type"
FT /evidence="ECO:0000259|PROSITE:PS51839"
FT DOMAIN 185..216
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 230..258
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 265..321
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 973 AA; 106392 MW; ACA5391BF670F519 CRC64;
MKDFIIPWDD RDMGTPAKAG KPVHLTIDGI DVTVPAGTSV MRAAMEAGIK VPKLCATDSV
EAFGSCRLCV VEIEGRRGTP ASCTTPVHAG MKVHTQSSKV KKIRKGVMEL YVSDHPLDCL
TCAANGDCEL QDMAGMVGLR DMRYTPGENH YDPSGTGARS QAEARLRMPE GEANPRYLPK
DESNPYFTYD PSKCIVCSRC VRACEEVQGT FALTIEGRGF ESRVSAGASG DDFLSSDCVS
CGACVQACPT ATLQEKSVAE LGTPDREVVT TCAYCGVGCS FKAELNGDQL VRMTPWKHGK
ANRGHSCVKG RFAYGYAEHP DRILNPMIRD SIDEPWREVS WPEALAFAAQ RMNGIREKYG
RRSLGVITSS RCTNEETYLV QKLTRAVFLN NNTDTCARVC HSPTGYGLGQ TFGTSAGTQD
FDSVEKVDVA LVIGANPTDG HPVFASRLKK RLREGAKLIV IDPRRIDMVK SAHIEAAHHL
PLTPGTNVAV VTALGHVIVT EGLYDEAFIR ERCDWDEFQA YAEFVSDKRH APESTALLTG
VNAQELRAAA RLFAKGGNGA IYYGLGVTEH SQGSTTVMAL ANLAMMTGNI GREGVGVNPL
RGQNNVQGSC DMGSFPHELP GYRHVKLPEV RKVFEDAWGV EIDPEPGLRI PNMLDAAVEG
TFKGLYCQGE DILQSDPDTR HVAAGLAAME CVIVHDLFLN ETANYAHVFL PGSSFLEKNG
TFTNAERRIN RVRKVMAPKN GYEDWEVTQL LANAMGAGWA YTHPEQIMAE IAATTPSFAG
VTYDLLEQKG SVQWPCNEEH PEGTPMMHVD GFMRGKGRFI VTEYVATAER SGPRFPLLLT
TGRILSQYNV GAQTRRTSNS VWHEQDLLEI HPHDAENRGL KDGDWIKLAS RSGETTLKAS
VTDKMSPGVV YTTFHHPDTQ ANVVTTDYSD WATNCPEYKV TAVQVSPSNG PTDWQEDYAA
QAERSRRILP AAE
//
