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Database: UniProt
Entry: A8JCP5_CHLRE
LinkDB: A8JCP5_CHLRE
Original site: A8JCP5_CHLRE 
ID   A8JCP5_CHLRE            Unreviewed;      1094 AA.
AC   A8JCP5;
DT   04-DEC-2007, integrated into UniProtKB/TrEMBL.
DT   04-DEC-2007, sequence version 1.
DT   27-MAR-2024, entry version 88.
DE   RecName: Full=proton-translocating NAD(P)(+) transhydrogenase {ECO:0000256|ARBA:ARBA00012943};
DE            EC=7.1.1.1 {ECO:0000256|ARBA:ARBA00012943};
GN   ORFNames=CHLRE_01g054500v5 {ECO:0000313|EMBL:PNW89009.1};
OS   Chlamydomonas reinhardtii (Chlamydomonas smithii).
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC   CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX   NCBI_TaxID=3055 {ECO:0000313|EMBL:PNW89009.1, ECO:0000313|Proteomes:UP000006906};
RN   [1] {ECO:0000313|EMBL:PNW89009.1, ECO:0000313|Proteomes:UP000006906}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CC-503 {ECO:0000313|Proteomes:UP000006906};
RX   PubMed=17932292; DOI=10.1126/science.1143609;
RA   Merchant S.S., Prochnik S.E., Vallon O., Harris E.H., Karpowicz S.J.,
RA   Witman G.B., Terry A., Salamov A., Fritz-Laylin L.K., Marechal-Drouard L.,
RA   Marshall W.F., Qu L.H., Nelson D.R., Sanderfoot A.A., Spalding M.H.,
RA   Kapitonov V.V., Ren Q., Ferris P., Lindquist E., Shapiro H., Lucas S.M.,
RA   Grimwood J., Schmutz J., Cardol P., Cerutti H., Chanfreau G., Chen C.L.,
RA   Cognat V., Croft M.T., Dent R., Dutcher S., Fernandez E., Fukuzawa H.,
RA   Gonzalez-Ballester D., Gonzalez-Halphen D., Hallmann A., Hanikenne M.,
RA   Hippler M., Inwood W., Jabbari K., Kalanon M., Kuras R., Lefebvre P.A.,
RA   Lemaire S.D., Lobanov A.V., Lohr M., Manuell A., Meier I., Mets L.,
RA   Mittag M., Mittelmeier T., Moroney J.V., Moseley J., Napoli C.,
RA   Nedelcu A.M., Niyogi K., Novoselov S.V., Paulsen I.T., Pazour G.,
RA   Purton S., Ral J.P., Riano-Pachon D.M., Riekhof W., Rymarquis L.,
RA   Schroda M., Stern D., Umen J., Willows R., Wilson N., Zimmer S.L.,
RA   Allmer J., Balk J., Bisova K., Chen C.J., Elias M., Gendler K., Hauser C.,
RA   Lamb M.R., Ledford H., Long J.C., Minagawa J., Page M.D., Pan J.,
RA   Pootakham W., Roje S., Rose A., Stahlberg E., Terauchi A.M., Yang P.,
RA   Ball S., Bowler C., Dieckmann C.L., Gladyshev V.N., Green P., Jorgensen R.,
RA   Mayfield S., Mueller-Roeber B., Rajamani S., Sayre R.T., Brokstein P.,
RA   Dubchak I., Goodstein D., Hornick L., Huang Y.W., Jhaveri J., Luo Y.,
RA   Martinez D., Ngau W.C., Otillar B., Poliakov A., Porter A., Szajkowski L.,
RA   Werner G., Zhou K., Grigoriev I.V., Rokhsar D.S., Grossman A.R.;
RT   "The Chlamydomonas genome reveals the evolution of key animal and plant
RT   functions.";
RL   Science 318:245-250(2007).
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}.
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DR   EMBL; CM008962; PNW89009.1; -; Genomic_DNA.
DR   RefSeq; XP_001700222.1; XM_001700170.1.
DR   AlphaFoldDB; A8JCP5; -.
DR   SMR; A8JCP5; -.
DR   STRING; 3055.A8JCP5; -.
DR   PaxDb; 3055-EDO98337; -.
DR   EnsemblPlants; PNW89009; PNW89009; CHLRE_01g054500v5.
DR   GeneID; 5725773; -.
DR   Gramene; PNW89009; PNW89009; CHLRE_01g054500v5.
DR   KEGG; cre:CHLRE_01g054500v5; -.
DR   eggNOG; ENOG502QQ0A; Eukaryota.
DR   HOGENOM; CLU_003376_0_0_1; -.
DR   InParanoid; A8JCP5; -.
DR   OMA; EQCREVD; -.
DR   OrthoDB; 313696at2759; -.
DR   Proteomes; UP000006906; Chromosome 1.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008746; F:NAD(P)+ transhydrogenase activity; IBA:GO_Central.
DR   GO; GO:0050661; F:NADP binding; IBA:GO_Central.
DR   GO; GO:0006740; P:NADPH regeneration; IBA:GO_Central.
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   Gene3D; 3.40.50.1220; TPP-binding domain; 1.
DR   InterPro; IPR008143; Ala_DH/PNT_CS2.
DR   InterPro; IPR007886; AlaDH/PNT_N.
DR   InterPro; IPR007698; AlaDH/PNT_NAD(H)-bd.
DR   InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR026255; NADP_transhyd_a.
DR   InterPro; IPR024605; NADP_transhyd_a_C.
DR   InterPro; IPR034300; PNTB-like.
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; PF02233; PNTB; 1.
DR   Pfam; PF12769; PNTB_4TM; 1.
DR   SMART; SM01002; AlaDh_PNT_C; 1.
DR   SMART; SM01003; AlaDh_PNT_N; 1.
DR   SUPFAM; SSF52467; DHS-like NAD/FAD-binding domain; 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   4: Predicted;
KW   Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   NAD {ECO:0000256|ARBA:ARBA00023027}; NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006906};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   DOMAIN          72..207
FT                   /note="Alanine dehydrogenase/pyridine nucleotide
FT                   transhydrogenase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01003"
FT   DOMAIN          216..381
FT                   /note="Alanine dehydrogenase/pyridine nucleotide
FT                   transhydrogenase NAD(H)-binding"
FT                   /evidence="ECO:0000259|SMART:SM01002"
SQ   SEQUENCE   1094 AA;  112347 MW;  1A869D2911A4122F CRC64;
     MLSMLGRKGQ AMCLRSSRQV PSTRASIARL LAQTPRPNVR ANALAGTAPG TSTSGPAEPI
     KDPIPYANLV VGVPRENAPG ERRVALSPAA VAGLLKQGFK TIVVEKGAGE YSQFTDAEYA
     SAGATLVDST EAMGADIVLR VRPPALEEVN KIKEGAVLVS YLYPARNKEL VEALAKRRAT
     AIGMDCIPRT ISRAQMFDSL SSMANIAGYR AVTEATQHFE RFLNGQITAA GRIPPAKVLV
     IGGGVAGLAA VGAAKSLGAI VRVFDTRTAV KEQAKSMGAE FLTVDIQEEG ESGTGYSKEM
     SPAFIEAEMK LFAAQAKEVD IIITTALIPG KGAPLLITKD MVDSMKPGSV IVDLSAEAGG
     NCGYTKPGEV VKTPNRVTVV GYTDMPSRMA GQSSTLYANN ISKLLLSAGP FTGGPKGHFR
     IDHADPVIRG SLVLEDGELR WPPPPGVIPQ ANTKVNETKD HKKDTGPVDL YEPTKRSALV
     TTGAVAAALA LGATSPSAAF SSMLTKFGLA SICGYQTVWG VVPALHSPLM SVTNAVSGLT
     AVGGMVLAGG GLLPGNTSQA LAGLAVAASA INIGGGFTIT QRMLDMFKRP TDPVEYNQLY
     ALPAATLVGG YVAASLFMGG TGGDPEGVTS ASYLASSAMC IAAIACLANQ SSARTGNALG
     MAGVGTGIAT TLGVMNAPAA VYAQVLTMLG AGIATGHYVG KTMKITELPQ MVAAFHSLVG
     LAAVVTSIAN VMAADPGHLD MTHKVIAYLG DFIGAVTMTG SAIAFGKLHG VLKSDPLSLP
     GKNAINLGLF AANLACGAAF LASDGSTDAG VLALVAAGVL AGVQGAHMTA SIGGADMPVV
     ITLLNSYSGY ALCAEGFLLN NDLLTAVGAL IGSSGAILSY IMCTAMNRSL PNVILGGYGM
     TAKAPADAAA VAGTHQEIDV GGVAEALTTA SKVIIVPGYG MAVANAQYPV AELAKHLTDK
     GISVKFGIHP VAGRMPGQLN VLLAEAGVPY DVVFEMDEIN EEIEEADVCL VIGANDTVNS
     AAVEDPNSVI AGMPVIEVWR SKQVFFMKRT MGAGYAGAEN PVFYKPNTFM FLGDAKKQTD
     ALLARVNETL GIKA
//
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