ID U2RLT3_9ACTN Unreviewed; 503 AA.
AC U2RLT3;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Putative NADH dehydrogenase subunit G {ECO:0000313|EMBL:ERK54493.1};
DE Flags: Fragment;
GN ORFNames=HMPREF0682_1460 {ECO:0000313|EMBL:ERK54493.1};
OS Propionibacterium acidifaciens F0233.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Propionibacteriaceae; Propionibacterium.
OX NCBI_TaxID=553198 {ECO:0000313|EMBL:ERK54493.1, ECO:0000313|Proteomes:UP000017052};
RN [1] {ECO:0000313|EMBL:ERK54493.1, ECO:0000313|Proteomes:UP000017052}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0233 {ECO:0000313|EMBL:ERK54493.1,
RC ECO:0000313|Proteomes:UP000017052};
RA Durkin A.S., Haft D.R., McCorrison J., Torralba M., Gillis M., Haft D.H.,
RA Methe B., Sutton G., Nelson K.E.;
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
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 -!- 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:ERK54493.1}.
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DR EMBL; ACVN02000214; ERK54493.1; -; Genomic_DNA.
DR AlphaFoldDB; U2RLT3; -.
DR OrthoDB; 9810782at2; -.
DR Proteomes; UP000017052; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro.
DR GO; GO:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro.
DR CDD; cd00207; fer2; 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; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR InterPro; IPR000283; NADH_UbQ_OxRdtase_75kDa_su_CS.
DR InterPro; IPR019574; NADH_UbQ_OxRdtase_Gsu_4Fe4S-bd.
DR PANTHER; PTHR43105:SF12; NADH-QUINONE OXIDOREDUCTASE SUBUNIT G; 1.
DR PANTHER; PTHR43105; RESPIRATORY NITRATE REDUCTASE; 1.
DR Pfam; PF13510; Fer2_4; 1.
DR Pfam; PF04879; Molybdop_Fe4S4; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF10588; NADH-G_4Fe-4S_3; 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; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS51839; 4FE4S_HC3; 1.
DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR PROSITE; PS00641; COMPLEX1_75K_1; 1.
DR PROSITE; PS00642; COMPLEX1_75K_2; 1.
DR PROSITE; PS00643; COMPLEX1_75K_3; 1.
PE 4: Predicted;
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:ARBA00022485}.
FT DOMAIN 10..93
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 95..134
FT /note="4Fe-4S His(Cys)3-ligated-type"
FT /evidence="ECO:0000259|PROSITE:PS51839"
FT DOMAIN 233..289
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
FT NON_TER 503
FT /evidence="ECO:0000313|EMBL:ERK54493.1"
SQ SEQUENCE 503 AA; 54839 MW; D3152DFF4752346D CRC64;
MSADVAAKPD TVTFTIDGTE VEVPKGTLVI RAAEMIGLEI PRFCDHPLLD PVAACRACLV
EVPDAGNGRP MKPQPACALA AMPGMRVETG ESNETVAKHQ RGMLEFLLIN HPLDCPICDK
GGECPLQNQT MSHGPGESRY EGAKRTYAKP IRISAEILLD RDRCVLCQRC TRFSNQISGD
DFISLAERGA MSQISGYEEQ PYFSYFAGNI VQICPVGALT SADYRFQSRP FDLVSTTTSC
ENCAAGCELR VDHRHYSVRR RLAGDDPAVN EEWNCDKGRF GYRSAQDGRR LTSPLVRRDG
ELVPAGWHEA IDAAAAGLRA AGAVGVLPGG RLTLENAYGW SRFARAVLDT DDIDFRARPV
SDEETSFLMA HVAGRSFDES VHYADLESAG RVVLVALEPE DECPIVFLRL RKAWRKRGLE
VVALAPFSSR GSRRTGARLW ATAPGQEAAR LAELAREGGI DERTIILVGE RAATSPGALS
EVVAQARAHG ARFAWIPRRA GEL
//
