ID S6BP39_PSERE Unreviewed; 1024 AA.
AC S6BP39;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE SubName: Full=Formate dehydrogenase alpha subunit {ECO:0000313|EMBL:BAN50804.1};
GN ORFNames=PCA10_50720 {ECO:0000313|EMBL:BAN50804.1};
OS Pseudomonas resinovorans NBRC 106553.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1245471 {ECO:0000313|EMBL:BAN50804.1, ECO:0000313|Proteomes:UP000015503};
RN [1] {ECO:0000313|EMBL:BAN50804.1, ECO:0000313|Proteomes:UP000015503}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 106553 {ECO:0000313|EMBL:BAN50804.1,
RC ECO:0000313|Proteomes:UP000015503};
RX PubMed=23887915; DOI=10.1128/genomeA.00488-13;
RA Shintani M., Hosoyama A., Ohji S., Tsuchikane K., Takarada H., Yamazoe A.,
RA Fujita N., Nojiri H.;
RT "Complete Genome Sequence of the Carbazole Degrader Pseudomonas
RT resinovorans Strain CA10 (NBRC 106553).";
RL Genome Announc. 1:e00488-13(2013).
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 -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|ARBA:ARBA00004418}.
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00010312}.
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DR EMBL; AP013068; BAN50804.1; -; Genomic_DNA.
DR STRING; 1245471.PCA10_50720; -.
DR KEGG; pre:PCA10_50720; -.
DR PATRIC; fig|1245471.3.peg.5144; -.
DR eggNOG; COG0243; Bacteria.
DR eggNOG; COG3383; Bacteria.
DR HOGENOM; CLU_000422_1_0_6; -.
DR OrthoDB; 9810782at2; -.
DR Proteomes; UP000015503; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:InterPro.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0047111; F:formate dehydrogenase (cytochrome-c-553) activity; IEA:InterPro.
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:InterPro.
DR CDD; cd02792; MopB_CT_Formate-Dh-Na-like; 1.
DR CDD; cd02752; MopB_Formate-Dh-Na-like; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.30.200.210; -; 1.
DR Gene3D; 3.40.50.740; -; 1.
DR Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 2.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR006443; Formate-DH-alph_fdnG.
DR InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR InterPro; IPR027467; MopterinOxRdtase_cofactor_BS.
DR InterPro; IPR006311; TAT_signal.
DR NCBIfam; TIGR01553; formate-DH-alph; 1.
DR PANTHER; PTHR43598:SF1; FORMATE DEHYDROGENASE, NITRATE-INDUCIBLE, MAJOR SUBUNIT; 1.
DR PANTHER; PTHR43598; TUNGSTEN-CONTAINING FORMYLMETHANOFURAN DEHYDROGENASE 2 SUBUNIT B; 1.
DR Pfam; PF04879; Molybdop_Fe4S4; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR SMART; SM00926; Molybdop_Fe4S4; 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.
DR PROSITE; PS00551; MOLYBDOPTERIN_PROK_1; 1.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
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 Molybdenum {ECO:0000256|ARBA:ARBA00022505};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000015503};
KW Selenium {ECO:0000313|EMBL:BAN50804.1};
KW Selenocysteine {ECO:0000313|EMBL:BAN50804.1};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 44..107
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
FT NON_STD 197
FT /note="Selenocysteine"
FT /evidence="ECO:0000313|EMBL:BAN50804.1"
SQ SEQUENCE 1024 AA; 113259 MW; EB6B35A07F6A4575 CRC64;
MDMNRRQFFK VCAVGLGGSS LAALGVAPPE AFADQVRHFR LARTIETRNT CPYCSVGCGL
IMHSQGDAAK NVAQNIIHIE GDADHPVNRG TLCPKGAGLL DFVHSPSRLK YPEVREPGSN
EWKRVGWDEA LDRIATLMKA DRDANFIEKN DQGQTVNRWL TTGFLAASAS SNEAGYITHK
VVRSLGMLGF DNQARVUHGP TVAGLAPTFG RGAMTNHWTD IKNADLVLIM GGNAAEAHPC
GFKWVTEAKA HNNARLIVVD PRFTRSASVA DYYAPIRTGT DIAFLGGLIN HLISHDRIQH
EYVRNYTDAS FIVNEGFSFE DGLFNGYDEA KRAYTDKASW SYAKGEDGFV RSDPTLQDPR
CVFQLMKQHY SRYTPDLVSS ICGTPKAQLD QVWGLVAETS DPRKTMTVMY ALGWTQHSVG
SQMIRTGAMV QLLLGNIGMP GGGMNALRGH SNIQGLTDLG LLSNSLPGYL TLASDAEQDY
AAYIDKRTSK PVRPGQLSYW QNYPKFHVSL MKSWFGKAAT VENNWCYDWL PKLDVPAYDV
LRYFDMMHQG KVNGYFCQGF NPIASFPNKA KVVASLGKLK FLVVMDPLAT ETSEFWRNAG
EFNDVDTASI QTTVFRLPTS CFAEEDGSLV NSGRWLQWHW KGAEPPGQAR TDIAIMGGLL
HRLRAAYTKD GGAFPDPILG LDWNYLRPDE PGPDEIAREF NGRALADLND PASGALLLKA
GEQLPGFAVL RDDGSTASGC WIFAGSWTAA GNQMARRDNA DPHAMGQTLG WAWAWPANRR
ILYNRASADL AGKPWNPEKK RLVWWNGKAW GGTDVPDFKA DSPPEAGMSP FIMNPEGVAR
FFALDKMNEG PFPEHYEPFE TPIGRNPLHP EHAKVTNNPA ARIFKGDWEM LGKADEFPYA
ATTYRLTEHF HFWTKHCKLN AITQPEQFVE ISEVLANELG IVAGERVKVS SNRGYIKAVA
VVTKRLKPLT VDGKTVHQVG IPLHWGFSGL ARNGYLTNTL TPFVGDGNTQ TPEFKSFLVK
VEKA
//
