ID X0QQ71_9GAMM Unreviewed; 466 AA.
AC X0QQ71;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 24-JAN-2024, entry version 26.
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=JCM18900_12261 {ECO:0000313|EMBL:GAF53672.1};
OS Psychrobacter sp. JCM 18900.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Psychrobacter.
OX NCBI_TaxID=1298608 {ECO:0000313|EMBL:GAF53672.1, ECO:0000313|Proteomes:UP000019500};
RN [1] {ECO:0000313|EMBL:GAF53672.1, ECO:0000313|Proteomes:UP000019500}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 18900 {ECO:0000313|EMBL:GAF53672.1,
RC ECO:0000313|Proteomes:UP000019500};
RA Kudo T., Kidera A., Kida M., Kawauchi A., Shimizu R., Nakahara T.,
RA Zhang X., Yamada A., Amano M., Hamada Y., Taniyama S., Arakawa O.,
RA Yoshida A., Oshima K., Suda W., Kuwahara H., Nogi Y., Kitamura K., Yuki M.,
RA Iida T., Moriya S., Inoue T., Hongo Y., Hattori M., Ohkuma M.;
RT "Draft Genome Sequences of Psychrobacter Strains JCM 18900, JCM 18901, JCM
RT 18902, and JCM 18903, Isolated Preferentially from Frozen Aquatic
RT Organisms.";
RL Genome Announc. 2:e00280-14(2014).
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:GAF53672.1}.
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; BAWG01000009; GAF53672.1; -; Genomic_DNA.
DR AlphaFoldDB; X0QQ71; -.
DR eggNOG; COG1282; Bacteria.
DR Proteomes; UP000019500; 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 14..30
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 64..81
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 93..115
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 127..149
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 161..182
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 188..207
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 14..459
FT /note="NADP transhydrogenase beta-like"
FT /evidence="ECO:0000259|Pfam:PF02233"
SQ SEQUENCE 466 AA; 49074 MW; AE5CC058000856B0 CRC64;
MNDFSTMIAA NADWFYLVGA ILFVLTLRGL SSPKTAIRGN RFGMAAMAIA VVTTFFLAEG
PVLWLIIGAM VLGALVGMWK AKTVAMTQMP ETVALMHSFV GLAAVAIALA TVLHTEQQHG
AVARIELFIG CFIGAITFSA SVFAFGKLAA KSWAKTLVGG WVKPVQALLF IAMIGFGGVY
FVTDSLPAFY AMAVIAVIFG WMWIAPIGGG DMPVVVSLLN SFSGWAAAGI GFTLGNSMLI
IAGSLVGSSG AILSYIMCKA MNRSLLNVLF GGMGTSAVAA GGDDGAPKNY KAGSAEDAGF
LMSNASSVVI VPGYGMAQGR AQNAVKELYE LLKEEGVNVR FAIHPVAGRM PGHMNVLLAE
ADVPYDDILE MDEINSDFAS TDVVLVIGAN DVVNPSAKDD PTSPIFGMPI LEVSKAQTVM
VIKRSMSTGY AGLDNSLFYM DKTMMIFGDA KKMVEEMVRT INGGGH
//
