ID F9ZV79_METMM Unreviewed; 517 AA.
AC F9ZV79;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=NAD(P) transhydrogenase subunit alpha {ECO:0000256|PIRNR:PIRNR000203};
DE EC=7.1.1.1 {ECO:0000256|PIRNR:PIRNR000203};
GN OrderedLocusNames=Metme_2285 {ECO:0000313|EMBL:AEG00689.1};
OS Methylomonas methanica (strain MC09).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Methylococcales;
OC Methylococcaceae; Methylomonas.
OX NCBI_TaxID=857087 {ECO:0000313|EMBL:AEG00689.1, ECO:0000313|Proteomes:UP000008888};
RN [1] {ECO:0000313|EMBL:AEG00689.1, ECO:0000313|Proteomes:UP000008888}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MC09 {ECO:0000313|EMBL:AEG00689.1,
RC ECO:0000313|Proteomes:UP000008888};
RX PubMed=22123758; DOI=10.1128/JB.06267-11;
RA Boden R., Cunliffe M., Scanlan J., Moussard H., Kits K.D., Klotz M.G.,
RA Jetten M.S., Vuilleumier S., Han J., Peters L., Mikhailova N., Teshima H.,
RA Tapia R., Kyrpides N., Ivanova N., Pagani I., Cheng J.F., Goodwin L.,
RA Han C., Hauser L., Land M.L., Lapidus A., Lucas S., Pitluck S., Woyke T.,
RA Stein L., Murrell J.C.;
RT "Complete Genome Sequence of the Aerobic Marine Methanotroph Methylomonas
RT methanica MC09.";
RL J. Bacteriol. 193:7001-7002(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=MC09;
RA Boden R., Cunliffe M., Scanlan J., Moussard H., Kits K.D., Klotz M.,
RA Jetten M., Vuilleumier S., Han J., Peters L., Mikhailova N., Teshima H.,
RA Tapia R., Kyrpides N., Ivanova N., Pagani I., Cheng J.-F., Goodwin L.,
RA Han C., Hauser L., Land M., Lapidus A., Lucas S., Pitluck S., Woyke T.,
RA Stein L.Y., Murrell C.;
RT "Complete genome sequence of the aerobic marine methanotroph Methylomonas
RT methanica MC09.";
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000008888}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MC09 {ECO:0000313|Proteomes:UP000008888};
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Teshima H., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Pagani I., Stein L., Woyke T.;
RT "Complete sequence of Methylomonas methanica MC09.";
RL Submitted (MAY-2011) 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:PIRNR000203}.
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:PIRNR000203};
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 AlaDH/PNT family.
CC {ECO:0000256|ARBA:ARBA00005689, ECO:0000256|PIRNR:PIRNR000203}.
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DR EMBL; CP002738; AEG00689.1; -; Genomic_DNA.
DR RefSeq; WP_013818930.1; NC_015572.1.
DR AlphaFoldDB; F9ZV79; -.
DR STRING; 857087.Metme_2285; -.
DR KEGG; mmt:Metme_2285; -.
DR eggNOG; COG3288; Bacteria.
DR HOGENOM; CLU_003376_2_1_6; -.
DR OrthoDB; 9804592at2; -.
DR Proteomes; UP000008888; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008746; F:NAD(P)+ transhydrogenase activity; IEA:InterPro.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:1902600; P:proton transmembrane transport; IEA:InterPro.
DR CDD; cd05304; Rubrum_tdh; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR InterPro; IPR008143; Ala_DH/PNT_CS2.
DR InterPro; IPR007886; AlaDH/PNT_N.
DR InterPro; IPR007698; AlaDH/PNT_NAD(H)-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR026255; NADP_transhyd_a.
DR InterPro; IPR024605; NADP_transhyd_a_C.
DR NCBIfam; TIGR00561; pntA; 1.
DR PANTHER; PTHR10160; NAD(P) TRANSHYDROGENASE; 1.
DR PANTHER; PTHR10160:SF19; PROTON-TRANSLOCATING NAD(P)(+) TRANSHYDROGENASE; 1.
DR Pfam; PF01262; AlaDh_PNT_C; 1.
DR Pfam; PF05222; AlaDh_PNT_N; 1.
DR Pfam; PF12769; PNTB_4TM; 1.
DR PIRSF; PIRSF000203; NADP_transhydrogenase_alpha; 1.
DR SMART; SM01002; AlaDh_PNT_C; 1.
DR SMART; SM01003; AlaDh_PNT_N; 1.
DR SUPFAM; SSF52283; Formate/glycerate dehydrogenase catalytic domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00837; ALADH_PNT_2; 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 NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|PIRNR:PIRNR000203};
KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|PIRNR:PIRNR000203};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR000203};
KW Reference proteome {ECO:0000313|Proteomes:UP000008888};
KW Translocase {ECO:0000256|ARBA:ARBA00022967, ECO:0000256|PIRNR:PIRNR000203};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 409..428
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 434..452
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 459..478
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 484..507
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 4..145
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01003"
FT DOMAIN 154..318
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase NAD(H)-binding"
FT /evidence="ECO:0000259|SMART:SM01002"
SQ SEQUENCE 517 AA; 55359 MW; 19DCEED11D87AB8E CRC64;
MKIGVPKEIH DGEKRVATTP EAADKIIKLG FKMCIESGAG LLANISDEAY REVGVEIVPD
AKAVWKDSDI VMKVRAPERH PELSTDEVEL MKDGQHLISF IWPAQNENLM KQLAAKNATV
LAMDSVPRMS RAQKMDALSS MANIAGYRAI VEAAQHFGRF FTGQITAAGK VPPAKVLVIG
AGVAGLAAIG AAKSMGAIVR AFDTRPEVKE QIESMDAEFL MLDFKEDGSG SGGYAKTMSK
EFIEAEMALF ARQAMEVDII ITTALIPGKP APELITAGMV KSMKPGSVIV DLAAEQGGNC
ALTEKDQIVV KHDVTIIGYT NLPSRLANQS SQLYATNLRH LLTDLCPGKD GVVNVNMEDE
VIRGATVIKE GAITWPPPPP KITASHKPLT ESPAVEVKPE KKKSLLGQFL PIVLAGAALF
GMGAVAPHSF LEHFTVFVLA CFVGYQVIWN VSASLHTPLM SVTNAISGII VIGALLQVST
PDNLVITLLS GVAILIAAIN ICGGFLVTRR MLEMFRK
//
