ID A0A1M7RLX5_9ACTN Unreviewed; 926 AA.
AC A0A1M7RLX5;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Formate dehydrogenase alpha subunit {ECO:0000313|EMBL:SHN47102.1};
GN ORFNames=SAMN05443668_12058 {ECO:0000313|EMBL:SHN47102.1};
OS Cryptosporangium aurantiacum.
OC Bacteria; Actinomycetota; Actinomycetes; Cryptosporangiales;
OC Cryptosporangiaceae; Cryptosporangium.
OX NCBI_TaxID=134849 {ECO:0000313|EMBL:SHN47102.1, ECO:0000313|Proteomes:UP000184440};
RN [1] {ECO:0000313|EMBL:SHN47102.1, ECO:0000313|Proteomes:UP000184440}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 46144 {ECO:0000313|EMBL:SHN47102.1,
RC ECO:0000313|Proteomes:UP000184440};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-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 -!- 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: In the C-terminal section; belongs to the prokaryotic
CC molybdopterin-containing oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00007023}.
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DR EMBL; FRCS01000020; SHN47102.1; -; Genomic_DNA.
DR RefSeq; WP_073264659.1; NZ_FRCS01000020.1.
DR AlphaFoldDB; A0A1M7RLX5; -.
DR STRING; 134849.SAMN05443668_12058; -.
DR OrthoDB; 7376058at2; -.
DR Proteomes; UP000184440; Unassembled WGS sequence.
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: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:UP000184440}.
FT DOMAIN 18..96
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 96..135
FT /note="4Fe-4S His(Cys)3-ligated-type"
FT /evidence="ECO:0000259|PROSITE:PS51839"
FT DOMAIN 158..189
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 200..229
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 236..292
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 926 AA; 99421 MW; 3ED6A048F74F99CB CRC64;
MTLLKEPDFG TPAKPGAPTV TIEVDGLPVA VPPDTSVMRA AAQAGVNIPK LCATDSLDAF
GSCRLCVVEI DGRRGTPASC TTPVGDGMRI RTQSPHLERL RRGVMELYLS DHPLDCLTCP
ANGDCELQDM AGEVGLREVR YGYDGANHLD APKDTSNPYF DFDESKCIAC SRCVRACDEI
QGTLALTIAN RGFASKVAPG PTSFLDSECV SCGACVQACP TATLQEKSVV ELGMPSRTVI
TTCAYCGVGC SFKAELRGTE LVRMVPHKDG GANEGHSCVK GRFAFGYATH PDRVLSPMVR
DSITDPWREV SWEFAIETVA RRFREIQGAH GPGSIGAISS SRCTNEEVYV VQKMVRAAFG
NNNVDTCARV CHSPTGYGLK QTFGESAGTQ DFKSVALADV ILVIGANPTD GHPVFASRMK
RRLRQGAQLI VVDPRRIDLV RSPHVEAAHH LQLRPGTNVA VVNALAHVVV TEGLVSRDFV
ASRCEGYDEW ATFIASPENS PEAVEGITGV PAATVRAAAR LYANAGNGTI YYGLGVTEHS
QGSTMVMGLA NLAMATGNVG RDGVGVNPLR GQNNVQGSCD MGSFPHELPG YRHVSDDVVR
ELFSARWGAP ILAEPGLRIP NMFDAAIDGS FRGLFVHGED IAQSDPNLSH VTAALSAIEL
VVVQDLFLNE TAKFAHVFLP GASFLEKDGT FTNAERRINR VRAVMPPKTG KSEWEIVCEI
ATAMGYPMAY SHPSEIMDEI AAMTPTFAGV SFEALDKLGS IQWPCNAAAP AGTPVMHVDS
FVRGRGKFVR TAYVATEEQT TRRFPLVLTT GRILSQYNVG AQTRRTGNVA WHPEDLLEIH
PHDASERGVS EGDLVRLASR VGETTLRATI SDRMPVGVVY TTFHHPVTGA NVVTTEHSDW
ATNCPEYKVT AVQVALVPAK LPSGVN
//
