ID A0A231HP52_9BURK Unreviewed; 956 AA.
AC A0A231HP52;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Formate dehydrogenase subunit alpha {ECO:0000313|EMBL:OXR50660.1};
GN ORFNames=PuT2_01990 {ECO:0000313|EMBL:OXR50660.1};
OS Pusillimonas sp. T2.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Pusillimonas.
OX NCBI_TaxID=1548123 {ECO:0000313|EMBL:OXR50660.1, ECO:0000313|Proteomes:UP000216496};
RN [1] {ECO:0000313|EMBL:OXR50660.1, ECO:0000313|Proteomes:UP000216496}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T2 {ECO:0000313|EMBL:OXR50660.1,
RC ECO:0000313|Proteomes:UP000216496};
RA Yuan M., Qiu J.G., Ma Y.;
RT "The genome sequence of Pusillimonas sp. T2.";
RL Submitted (JUN-2017) 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 -!- 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:OXR50660.1}.
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DR EMBL; NIQA01000001; OXR50660.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A231HP52; -.
DR OrthoDB; 9810782at2; -.
DR Proteomes; UP000216496; 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:UP000216496}.
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 161..192
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 204..233
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 240..296
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 956 AA; 105253 MW; 14AB1D8F1D88E3CC CRC64;
MLETIAKRDR DFGTPARVST QLVNLTIDGQ TIQVPEGTSV MRAAAEMGIN IPKLCATDSL
EAFGSCRLCL VHIEGRRGFP ASCTTPVEEG MVVITENKKL NDMRRNVMEL YISDHPLDCL
TCPANGDCEL QDMAGVVGLR NVRYGYDGAN HLNDATDASN PYFAYDPSKC IVCSRCVRAC
EDIQGTFALT IDSKGFESRI TAGQKDTFLE SDCVSCGACV QACPTSSLME KTVIMMGQPE
HSVVTTCAYC GVGCAFKADM KGQEVVRMVP WKDGKANRGH SCVKGRFAWG YATHKDRVLK
PMIREKITDP WREVSWEEAI GYAASQIRRI QNQYGRDSVG GITSSRCTNE ETYLVQKLVR
AAFGTNNVDT CARVCHSPTG YGLKTTLGES AGTQTFDSVM HTDVVIVMGA NPSAAHPVFA
SRLKSRLRQG AKLIVIDPRT IELVSSPHIK ADYHLPVRPG TNTALLTSMA HVIATENLID
EAFVAERCET KAFNEWREFV SRPENSPEAM AEITGVNADD LRGAARLFAT HGNGSIYYGL
GVTEHSQGST TVMAIANLAM ATGNIGREGV GVNPLRGQNN VQGSCDMGSF PHELPGYRHV
SDDTVRRQFE QAWGVTIQPE PGLRIPNMFD AALSGSFKAL YCQGEDIVQS DPNTQHVTAA
LSAMECIIVQ DIFLNETAKY AHVFLPGSSF LEKDGTFTNA ERRISRVRQV MEPQAGLADW
EATCALSNAL GYPMNYKHPS EIMDEIASLT PTFTGVSFKR IDELGGSVQW PCNEDAPEGT
PIMHIDQFVR GKGKFVITQY VPSDERSTRK FPLLLTTGRI LSQYNVGAQT RRTDNVMWHH
EDVLEIHPHD AEERGINVGD WVAVQSRSGE TALRAEITDR VQPGVVYTTF HHPESGANVV
TTDSSDWATD CPEYKVTAVQ VRRVTQPSDW QTHWTRFTDM QHDLLEKRIK EPAPSN
//
