ID H8IJC0_MYCIA Unreviewed; 474 AA.
AC H8IJC0;
DT 16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2012, sequence version 1.
DT 27-MAR-2024, entry version 46.
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 OrderedLocusNames=OCU_49600 {ECO:0000313|EMBL:AFC46179.1};
OS Mycobacterium intracellulare (strain ATCC 13950 / DSM 43223 / JCM 6384 /
OS NCTC 13025 / 3600).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium avium complex (MAC).
OX NCBI_TaxID=487521 {ECO:0000313|EMBL:AFC46179.1, ECO:0000313|Proteomes:UP000008004};
RN [1] {ECO:0000313|EMBL:AFC46179.1, ECO:0000313|Proteomes:UP000008004}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13950 / DSM 43223 / JCM 6384 / NCTC 13025 / 3600
RC {ECO:0000313|Proteomes:UP000008004};
RX PubMed=22535933; DOI=10.1128/JB.00295-12;
RA Kim B.J., Choi B.S., Lim J.S., Choi I.Y., Lee J.H., Chun J., Kook Y.H.,
RA Kim B.J.;
RT "Complete genome sequence of Mycobacterium intracellulare strain ATCC
RT 13950T.";
RL J. Bacteriol. 194:2750-2750(2012).
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}.
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DR EMBL; CP003322; AFC46179.1; -; Genomic_DNA.
DR RefSeq; WP_009956633.1; NZ_CP076382.1.
DR AlphaFoldDB; H8IJC0; -.
DR GeneID; 77299580; -.
DR KEGG; mia:OCU_49600; -.
DR PATRIC; fig|487521.10.peg.4967; -.
DR eggNOG; COG1282; Bacteria.
DR HOGENOM; CLU_007866_4_0_11; -.
DR Proteomes; UP000008004; 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 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 Oxidoreductase {ECO:0000313|EMBL:AFC46179.1};
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 6..25
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 32..51
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 57..74
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 86..103
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 123..147
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 168..189
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 195..217
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 224..244
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 250..268
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 8..469
FT /note="NADP transhydrogenase beta-like"
FT /evidence="ECO:0000259|Pfam:PF02233"
SQ SEQUENCE 474 AA; 48392 MW; F0C2AE29A9AD1E53 CRC64;
MNYLVIGLYI ISFALFIYGL MGLTGPKTAV RGNLIAAVGM AIAVAATLVK IRHTDQWVLI
IAGLVVGVVL GVPPARYTKM TAMPQLVAFF NGVGGGTVAL IALSEFIETQ GFSAFQHGES
PTVHIVVASL FAAVIGSISF WGSIIAFGKL QEIISGAPIG FGRAQQPVNL LLLVAAVAAA
VVVGVHAHPG TGGASLWWMI GLLAAAGVLG LMVVLPIGGA DMPVVISLLN AMTGLSAAAA
GLALNNTAMI VAGMIVGASG SILTNLMAKA MNRSIPAIVA GGFGGGGVAP SGDGGGDKTV
KATSAADAAI QMAYANQVIV VPGYGLAVAQ AQHAVKDMAA LLEDKGVEVK YAIHPVAGRM
PGHMNVLLAE AEVDYDAMKD MDDINDEFAR TDVAIVIGAN DVTNPAARND ASSPIYGMPI
LNVDKAKSVI VLKRSMNSGF AGIDNPLFYG EGTSMLFGDA KKSVTEVAEE LKAL
//
