ID N9MDW8_9GAMM Unreviewed; 481 AA.
AC N9MDW8;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=NAD(P) transhydrogenase subunit beta {ECO:0000256|ARBA:ARBA00014581, ECO:0000256|PIRNR:PIRNR000204};
DE EC=7.1.1.1 {ECO:0000256|ARBA:ARBA00012943, ECO:0000256|PIRNR:PIRNR000204};
DE AltName: Full=Nicotinamide nucleotide transhydrogenase subunit beta {ECO:0000256|PIRNR:PIRNR000204};
GN ORFNames=F905_01888 {ECO:0000313|EMBL:ENW88891.1};
OS Acinetobacter sp. CIP 53.82.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1144671 {ECO:0000313|EMBL:ENW88891.1, ECO:0000313|Proteomes:UP000018455};
RN [1] {ECO:0000313|EMBL:ENW88891.1, ECO:0000313|Proteomes:UP000018455}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIP 53.82 {ECO:0000313|EMBL:ENW88891.1,
RC ECO:0000313|Proteomes:UP000018455};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Cerqueira G., Feldgarden M., Courvalin P., Perichon B.,
RA Grillot-Courvalin C., Clermont D., Rocha E., Yoon E.-J., Nemec A.,
RA Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B.,
RA Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Larimer J., McCowan C., Murphy C., Neiman D., Pearson M.,
RA Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Acinetobacter sp. CIP 53.82.";
RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: The transhydrogenation between NADH and NADP is coupled to
CC respiration and ATP hydrolysis and functions as a proton pump across
CC the membrane. {ECO:0000256|ARBA:ARBA00003943,
CC ECO:0000256|PIRNR:PIRNR000204}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+)(in) + NAD(+) + NADPH = H(+)(out) + NADH + NADP(+);
CC Xref=Rhea:RHEA:47992, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:57945, ChEBI:CHEBI:58349; EC=7.1.1.1;
CC Evidence={ECO:0000256|ARBA:ARBA00000006,
CC ECO:0000256|PIRNR:PIRNR000204};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004429}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the PNT beta subunit family.
CC {ECO:0000256|ARBA:ARBA00007919, ECO:0000256|PIRNR:PIRNR000204}.
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:ENW88891.1}.
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DR EMBL; APRK01000011; ENW88891.1; -; Genomic_DNA.
DR RefSeq; WP_005180098.1; NZ_KB850046.1.
DR AlphaFoldDB; N9MDW8; -.
DR GeneID; 69466795; -.
DR PATRIC; fig|1144671.3.peg.1823; -.
DR HOGENOM; CLU_007866_4_0_6; -.
DR Proteomes; UP000018455; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008750; F:NAD(P)+ transhydrogenase (AB-specific) activity; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR Gene3D; 3.40.50.1220; TPP-binding domain; 1.
DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR InterPro; IPR012136; NADH_DH_b.
DR InterPro; IPR034300; PNTB-like.
DR PANTHER; PTHR44758; NAD(P) TRANSHYDROGENASE SUBUNIT BETA; 1.
DR PANTHER; PTHR44758:SF1; NAD(P) TRANSHYDROGENASE SUBUNIT BETA; 1.
DR Pfam; PF02233; PNTB; 1.
DR PIRSF; PIRSF000204; PNTB; 1.
DR SUPFAM; SSF52467; DHS-like NAD/FAD-binding domain; 1.
PE 3: Inferred from homology;
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519,
KW ECO:0000256|PIRNR:PIRNR000204};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475,
KW ECO:0000256|PIRNR:PIRNR000204};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR000204};
KW NAD {ECO:0000256|PIRNR:PIRNR000204};
KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|PIRNR:PIRNR000204};
KW Translocase {ECO:0000256|ARBA:ARBA00022967, ECO:0000256|PIRNR:PIRNR000204};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..26
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 38..54
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 60..77
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 89..109
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 137..158
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 178..195
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 201..220
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 227..245
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 251..271
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 10..474
FT /note="NADP transhydrogenase beta-like"
FT /evidence="ECO:0000259|Pfam:PF02233"
SQ SEQUENCE 481 AA; 51024 MW; FFB5FE1DBFE0AC67 CRC64;
MEFIRDYADW FYLIGAVLFI LTLRGLSGPK TAIAGNRYGM IAMAIAVLTT FFVADHPVIW
MIVGAMILGA IVGIARARTV PMTQMPETVA LMHSLVGLAA VLIAIAAIIH NNKLVELGPE
LLAANGVSFH EMSKVHLFEL FVGCFVGAIT FTASVFAYGK LAAKKWAKTI SGGWVKPVQA
LIFIAMLGFG IHFFLSGSMT SFWAMTALAL AFGWVWIAPV GGGDMPVVVS LLNSFSGWAA
AGIGFTLENN MLIVAGSLVG SSGAILSYIM CKAMNRSIIN VLFGGAMGGA AAPTAGAGEQ
VQRNYRSGSA DDAGFLMSNA DSVVIVPGYG MAQGRAQNAV KELANLLKEQ GVTVRFAIHP
VAGRMPGHMN VLLAEADVPY EDILEMDEIN SDFPATDVVL VIGANDVVNP AAKDDPNSPI
YGMPILEAHK ARTIMVIKRS MATGYAGLDN DLFYNDKTMM VFGDAKKVVE DMTKAINGTG
H
//
