ID A7I7X4_METB6 Unreviewed; 460 AA.
AC A7I7X4;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE RecName: Full=NAD(P) transhydrogenase subunit beta {ECO:0000256|ARBA:ARBA00014581};
DE EC=7.1.1.1 {ECO:0000256|ARBA:ARBA00012943};
DE AltName: Full=Nicotinamide nucleotide transhydrogenase subunit beta {ECO:0000256|ARBA:ARBA00033258};
DE AltName: Full=Pyridine nucleotide transhydrogenase subunit beta {ECO:0000256|ARBA:ARBA00030053};
GN OrderedLocusNames=Mboo_1317 {ECO:0000313|EMBL:ABS55835.1};
OS Methanoregula boonei (strain DSM 21154 / JCM 14090 / 6A8).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanomicrobiales; Methanoregulaceae; Methanoregula.
OX NCBI_TaxID=456442 {ECO:0000313|EMBL:ABS55835.1, ECO:0000313|Proteomes:UP000002408};
RN [1] {ECO:0000313|Proteomes:UP000002408}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21154 / JCM 14090 / 6A8
RC {ECO:0000313|Proteomes:UP000002408};
RX PubMed=25998264; DOI=10.1099/mic.0.000117;
RA Braeuer S., Cadillo-Quiroz H., Kyrpides N., Woyke T., Goodwin L.,
RA Detter C., Podell S., Yavitt J.B., Zinder S.H.;
RT "Genome of Methanoregula boonei 6A8 reveals adaptations to oligotrophic
RT peatland environments.";
RL Microbiology 161:1572-1581(2015).
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 -!- 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 -!- 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}.
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; CP000780; ABS55835.1; -; Genomic_DNA.
DR RefSeq; WP_012106868.1; NC_009712.1.
DR AlphaFoldDB; A7I7X4; -.
DR STRING; 456442.Mboo_1317; -.
DR GeneID; 5411776; -.
DR KEGG; mbn:Mboo_1317; -.
DR eggNOG; arCOG09400; Archaea.
DR HOGENOM; CLU_007866_4_0_2; -.
DR OrthoDB; 302282at2157; -.
DR Proteomes; UP000002408; Chromosome.
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 Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Reference proteome {ECO:0000313|Proteomes:UP000002408};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..24
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 36..53
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 59..77
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 89..112
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 118..138
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 159..179
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 185..205
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 212..231
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 237..255
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 11..455
FT /note="NADP transhydrogenase beta-like"
FT /evidence="ECO:0000259|Pfam:PF02233"
SQ SEQUENCE 460 AA; 48436 MW; F9FB7094E4BC9357 CRC64;
MIDFAWLIDP VYIVTIFFFI IGMYRMSHPL TARSGIVWAG AAMLIATLAT FLTANLNNIA
LMAIAIVIGG GFGYIAAKRV AMTGMPQMVA LFNGMGGGAA AGISAVELLG TIDVTSSLAI
IGGIIGAVSF AGSIIAFMKL QGWMRPRPVT FPGQQIVNTA VLVLAILSGA FIILTPAWLP
LGIATYLPLF FVLSLLFGVL MTLPIGGADM PVVISMYNAF TGLAVALDGF SFATPNYAMV
VAGIIVGAAG SLLTLQMAKA MNRSITNVFF GAFGATEEDG ATIQGSMKPI EADDVAVMLA
YADKVVVAPG YGMAVAQAQQ KVKELADLLE SRGVTVKFAI HPVAGRMPGH MNVLLAEAGV
AYDKLFDRDE INPEFAGTDV VLVIGANDTV NPASHRQGSP LYGMPVLDVE QAKNVIVLKR
GQGRGFAGIE NDLFYRDNTR LLYGDAQETV AKVVTALKKL
//
