ID D7FC64_HELP3 Unreviewed; 844 AA.
AC D7FC64;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE SubName: Full=NADH dehydrogenase I chain G {ECO:0000313|EMBL:CBI65771.1};
DE EC=1.6.5.3 {ECO:0000313|EMBL:CBI65771.1};
GN OrderedLocusNames=HPB8_214 {ECO:0000313|EMBL:CBI65771.1};
OS Helicobacter pylori (strain B8).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=693745 {ECO:0000313|EMBL:CBI65771.1, ECO:0000313|Proteomes:UP000007091};
RN [1] {ECO:0000313|EMBL:CBI65771.1, ECO:0000313|Proteomes:UP000007091}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B8 {ECO:0000313|EMBL:CBI65771.1,
RC ECO:0000313|Proteomes:UP000007091};
RX PubMed=20507619; DOI=10.1186/1471-2164-11-335;
RA Farnbacher M., Jahns T., Willrodt D., Daniel R., Haas R., Goesmann A.,
RA Kurtz S., Rieder G.;
RT "Sequencing, annotation, and comparative genome analysis of the gerbil-
RT adapted Helicobacter pylori strain B8.";
RL BMC Genomics 11:335-335(2010).
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FN598874; CBI65771.1; -; Genomic_DNA.
DR RefSeq; WP_000632192.1; NC_014256.1.
DR AlphaFoldDB; D7FC64; -.
DR KEGG; hpl:HPB8_214; -.
DR HOGENOM; CLU_021910_0_0_7; -.
DR Proteomes; UP000007091; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd00207; fer2; 1.
DR Gene3D; 3.10.20.740; -; 1.
DR Gene3D; 3.30.70.20; -; 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; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR InterPro; IPR019574; NADH_UbQ_OxRdtase_Gsu_4Fe4S-bd.
DR PANTHER; PTHR24960:SF88; PHOTOSYSTEM I IRON-SULFUR CENTER; 1.
DR PANTHER; PTHR24960; PHOTOSYSTEM I IRON-SULFUR CENTER-RELATED; 1.
DR Pfam; PF13510; Fer2_4; 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; 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 4: Predicted;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000313|EMBL:CBI65771.1};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 1..76
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 76..115
FT /note="4Fe-4S His(Cys)3-ligated-type"
FT /evidence="ECO:0000259|PROSITE:PS51839"
FT DOMAIN 134..163
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 193..223
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 232..291
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
FT REGION 470..510
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 480..510
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 844 AA; 94348 MW; EB5F7E97F4979BAE CRC64;
MITMNINGKT IECQEGQSVL EVARSAGIYI PTICYLSGCS PTVACKMCMV EMDGKRIYSC
NTKAKNNATI LTNTPTLMDE RKSIMQTYDV NHPLECGVCD KSGECELQDM THLTGVEHQP
YAVADDFKAL DSWAKALYDP NLCIMCERCV TTCKDNVGEN NLKATKADLH APDKFKDSMS
KDAFSVWSRK QKGIISFVGS VPCYDCGECI AVCPVGALSY KDFAYTANAW ELKKIHSTCS
HCSAGCLISY DVRHFDTLGE ESKIFRVLND FYHNPICGAG RFAFDVSSSP KGSTNLKEAQ
NALKECEAVR IGGDITNEEA FLIERLRKEL DFKIYNQEVY HFQQFLKVLG EVKRPNIEEI
KTSNLVVTIG SSIKTENPLV RYAINNALKL NKASLIAMHP IKDNALANLC RSSFCITHEV
GAEEILLGML LKMLNIESTA LKSLEDSKQS IVDEAALKAL EEERKKALEQ ANQGCSLEES
KAENQEEDKI EAAAPKEENP EENKTEVKEE KIEVPTKTTY LLLEEAGINL ETYEKILALL
QKSNNTLLVV GEEIYSHKQA HNIAKMLRLL AQKSAVKLIL IPPSTNALGI ASICQLSEEV
FEHEKIVGIR AQGDFTINSD DRVFGKDALS KVDFILPSLN QLEGTITNVE GRVLPLKPAL
RFEGYDLSDI MQGFGFVEEN LTECTHKLPT EAGFKAIEFD YLTNYFTNDR VNHRGYLLGT
SHFEKSAKEC ETIECEPIKP LKEKIAFNAY LKYPETQFNN ATNKSENLQL KAGVYVSKAF
LKKLNKEVGQ NITLFKEEEE LTGVLYLDES LDQEVFVISP SLLTNHSNFF REGVFDSVDL
KEQA
//
