ID A0A109LSM5_9SPHN Unreviewed; 663 AA.
AC A0A109LSM5;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=NADH-ubiquinone oxidoreductase chain 5 {ECO:0000256|ARBA:ARBA00021096};
DE EC=7.1.1.2 {ECO:0000256|ARBA:ARBA00012944};
GN ORFNames=AUC45_02605 {ECO:0000313|EMBL:KWV93038.1};
OS Erythrobacter sp. YT30.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Erythrobacter/Porphyrobacter group; Erythrobacter.
OX NCBI_TaxID=1735012 {ECO:0000313|EMBL:KWV93038.1, ECO:0000313|Proteomes:UP000055668};
RN [1] {ECO:0000313|EMBL:KWV93038.1, ECO:0000313|Proteomes:UP000055668}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YT30 {ECO:0000313|EMBL:KWV93038.1,
RC ECO:0000313|Proteomes:UP000055668};
RA Lin W., Zheng Q.;
RT "Draft genome sequence of Erythrobacter sp. YT30.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) +
CC NAD(+); Xref=Rhea:RHEA:29091, Rhea:RHEA-COMP:9565, Rhea:RHEA-
CC COMP:9566, ChEBI:CHEBI:15378, ChEBI:CHEBI:16389, ChEBI:CHEBI:17976,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=7.1.1.2;
CC Evidence={ECO:0000256|ARBA:ARBA00000766};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141,
CC ECO:0000256|RuleBase:RU000320}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU000320}.
CC Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004448}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004448}.
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:KWV93038.1}.
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DR EMBL; LMAF01000001; KWV93038.1; -; Genomic_DNA.
DR RefSeq; WP_067597710.1; NZ_LMAF01000001.1.
DR AlphaFoldDB; A0A109LSM5; -.
DR STRING; 1735012.AUC45_02605; -.
DR OrthoDB; 9811798at2; -.
DR Proteomes; UP000055668; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:UniProtKB-EC.
DR GO; GO:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro.
DR Gene3D; 1.20.5.2700; -; 1.
DR InterPro; IPR010934; NADH_DH_su5_C.
DR InterPro; IPR018393; NADHpl_OxRdtase_5_subgr.
DR InterPro; IPR001750; ND/Mrp_mem.
DR InterPro; IPR003945; NU5C-like.
DR InterPro; IPR001516; Proton_antipo_N.
DR NCBIfam; TIGR01974; NDH_I_L; 1.
DR PANTHER; PTHR42829; NADH-UBIQUINONE OXIDOREDUCTASE CHAIN 5; 1.
DR PANTHER; PTHR42829:SF2; NADH-UBIQUINONE OXIDOREDUCTASE CHAIN 5; 1.
DR Pfam; PF06455; NADH5_C; 1.
DR Pfam; PF00361; Proton_antipo_M; 1.
DR Pfam; PF00662; Proton_antipo_N; 1.
DR PRINTS; PR01434; NADHDHGNASE5.
DR PRINTS; PR01435; NPOXDRDTASE5.
PE 4: Predicted;
KW Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792};
KW Reference proteome {ECO:0000313|Proteomes:UP000055668};
KW Respiratory chain {ECO:0000256|ARBA:ARBA00022660};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU000320};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022660};
KW Ubiquinone {ECO:0000256|ARBA:ARBA00023075, ECO:0000313|EMBL:KWV93038.1}.
FT TRANSMEM 6..25
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 37..59
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 83..104
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 116..133
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 139..158
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 170..192
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 212..235
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 256..273
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 285..302
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 314..336
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 383..409
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 429..449
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 490..511
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 541..561
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 643..662
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 67..117
FT /note="NADH-Ubiquinone oxidoreductase (complex I) chain 5
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00662"
FT DOMAIN 133..430
FT /note="NADH:quinone oxidoreductase/Mrp antiporter membrane
FT subunit"
FT /evidence="ECO:0000259|Pfam:PF00361"
FT DOMAIN 532..659
FT /note="NADH dehydrogenase subunit 5 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF06455"
SQ SEQUENCE 663 AA; 72395 MW; 5284DEAD25631C82 CRC64;
MSPILIIVFA PLIAAIIAGF GNRALGNTGA KVVTTGALFL SAILSWPIFI AFLTGDAIAE
VVPVLKWVQS GEMTFDWELR VDALTAVMLV VINTVSALVH LYSWGYMEED PDQPRFFAYL
SLFTFAMLML VTADNLVQMF FGWEGVGLAS YLLIGFWFKK PSAGAAAIKA FVVNRVGDLG
FMLGIFGTYL VFKTTSIPEI LDAAPAMSGA TIGFLGMRLQ TMDVLCILLF IGAMGKSAQL
GLHTWLPDAM EGPTPVSALI HAATMVTAGV FMLCRLSPMF ETAPTALMVV TVTGGATCFF
AATIGTTQWD IKRVIAYSTC SQLGYMFFAA GVGAYGVAMF HLFTHAFFKA LLFLGAGSVI
HAMHHEQDMR YYGGLRKHIP ITFWAMMAGT LAITGLGVYH LGVGFAGFWS KDAILEVAFA
RGTGLSVTAF WLGVTAALLT SFYSWRLMFL TFWGKPRWIE SEHIQHSVHK TPEEAGEDTT
GGYHPHESPL TMLVPLGLLT VGAVLAGQVF APSFLDDAAF WDGSVFYNAN LIAAMHAVPY
WVKYSALIVM ILGFAGAYLA YIAKPDIPAK FVGTFGWLHN FVFRKWYFDE LYDRIFVKPA
FWFGRQFWKL GDIGTIDRFG PNGIAAVVQR GSVAAKSIQS GYLYTYALIM LLGLIAAVTY
VLL
//