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Database: UniProt
Entry: A0A109LSM5_9SPHN
LinkDB: A0A109LSM5_9SPHN
Original site: A0A109LSM5_9SPHN 
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
//
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