ID A9S190_PHYPA Unreviewed; 571 AA.
AC A9S190;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 24-JAN-2024, entry version 91.
DE RecName: Full=Aldehyde dehydrogenase domain-containing protein {ECO:0000259|Pfam:PF00171};
GN ORFNames=PHYPA_007260 {ECO:0000313|EMBL:PNR53585.1};
OS Physcomitrium patens (Spreading-leaved earth moss) (Physcomitrella patens).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Bryophyta;
OC Bryophytina; Bryopsida; Funariidae; Funariales; Funariaceae; Physcomitrium.
OX NCBI_TaxID=3218 {ECO:0000313|EMBL:PNR53585.1};
RN [1] {ECO:0000313|EMBL:PNR53585.1, ECO:0000313|Proteomes:UP000006727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Gransden 2004 {ECO:0000313|EnsemblPlants:Pp3c5_4940V3.1,
RC ECO:0000313|Proteomes:UP000006727};
RX PubMed=18079367; DOI=10.1126/science.1150646;
RA Rensing S.A., Lang D., Zimmer A.D., Terry A., Salamov A., Shapiro H.,
RA Nishiyama T., Perroud P.-F., Lindquist E.A., Kamisugi Y., Tanahashi T.,
RA Sakakibara K., Fujita T., Oishi K., Shin-I T., Kuroki Y., Toyoda A.,
RA Suzuki Y., Hashimoto S.-I., Yamaguchi K., Sugano S., Kohara Y.,
RA Fujiyama A., Anterola A., Aoki S., Ashton N., Barbazuk W.B., Barker E.,
RA Bennetzen J.L., Blankenship R., Cho S.H., Dutcher S.K., Estelle M.,
RA Fawcett J.A., Gundlach H., Hanada K., Heyl A., Hicks K.A., Hughes J.,
RA Lohr M., Mayer K., Melkozernov A., Murata T., Nelson D.R., Pils B.,
RA Prigge M., Reiss B., Renner T., Rombauts S., Rushton P.J., Sanderfoot A.,
RA Schween G., Shiu S.-H., Stueber K., Theodoulou F.L., Tu H., Van de Peer Y.,
RA Verrier P.J., Waters E., Wood A., Yang L., Cove D., Cuming A.C., Hasebe M.,
RA Lucas S., Mishler B.D., Reski R., Grigoriev I.V., Quatrano R.S.,
RA Boore J.L.;
RT "The Physcomitrella genome reveals evolutionary insights into the conquest
RT of land by plants.";
RL Science 319:64-69(2008).
RN [2] {ECO:0000313|EMBL:PNR53585.1, ECO:0000313|Proteomes:UP000006727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Gransden 2004 {ECO:0000313|EnsemblPlants:Pp3c5_4940V3.1,
RC ECO:0000313|Proteomes:UP000006727};
RX PubMed=29237241; DOI=10.1111/tpj.13801;
RA Lang D., Ullrich K.K., Murat F., Fuchs J., Jenkins J., Haas F.B.,
RA Piednoel M., Gundlach H., Van Bel M., Meyberg R., Vives C., Morata J.,
RA Symeonidi A., Hiss M., Muchero W., Kamisugi Y., Saleh O., Blanc G.,
RA Decker E.L., van Gessel N., Grimwood J., Hayes R.D., Graham S.W.,
RA Gunter L.E., McDaniel S.F., Hoernstein S.N.W., Larsson A., Li F.W.,
RA Perroud P.F., Phillips J., Ranjan P., Rokshar D.S., Rothfels C.J.,
RA Schneider L., Shu S., Stevenson D.W., Thummler F., Tillich M.,
RA Villarreal Aguilar J.C., Widiez T., Wong G.K., Wymore A., Zhang Y.,
RA Zimmer A.D., Quatrano R.S., Mayer K.F.X., Goodstein D., Casacuberta J.M.,
RA Vandepoele K., Reski R., Cuming A.C., Tuskan G.A., Maumus F., Salse J.,
RA Schmutz J., Rensing S.A.;
RT "The Physcomitrella patens chromosome-scale assembly reveals moss genome
RT structure and evolution.";
RL Plant J. 93:515-533(2018).
RN [3] {ECO:0000313|EnsemblPlants:Pp3c5_4940V3.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (DEC-2020) to UniProtKB.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00009986}.
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DR EMBL; ABEU02000005; PNR53585.1; -; Genomic_DNA.
DR RefSeq; XP_001760169.1; XM_001760117.1.
DR AlphaFoldDB; A9S190; -.
DR STRING; 3218.A9S190; -.
DR PaxDb; 3218-PP1S41_177V6-1; -.
DR EnsemblPlants; Pp3c5_4940V3.1; Pp3c5_4940V3.1; Pp3c5_4940.
DR EnsemblPlants; Pp3c5_4940V3.2; Pp3c5_4940V3.2; Pp3c5_4940.
DR Gramene; Pp3c5_4940V3.1; Pp3c5_4940V3.1; Pp3c5_4940.
DR Gramene; Pp3c5_4940V3.2; Pp3c5_4940V3.2; Pp3c5_4940.
DR eggNOG; KOG2451; Eukaryota.
DR HOGENOM; CLU_039242_0_0_1; -.
DR InParanoid; A9S190; -.
DR OMA; VDYVAWQ; -.
DR OrthoDB; 5485397at2759; -.
DR Proteomes; UP000006727; Chromosome 5.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0003842; F:1-pyrroline-5-carboxylate dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; IEA:InterPro.
DR GO; GO:0010133; P:proline catabolic process to glutamate; IBA:GO_Central.
DR GO; GO:0072593; P:reactive oxygen species metabolic process; IEA:EnsemblPlants.
DR GO; GO:0009651; P:response to salt stress; IEA:EnsemblPlants.
DR CDD; cd07126; ALDH_F12_P5CDH; 1.
DR InterPro; IPR016161; Ald_DH/histidinol_DH.
DR InterPro; IPR016163; Ald_DH_C.
DR InterPro; IPR016160; Ald_DH_CS_CYS.
DR InterPro; IPR016162; Ald_DH_N.
DR InterPro; IPR015590; Aldehyde_DH_dom.
DR InterPro; IPR044638; ALDH7A1-like.
DR PANTHER; PTHR43521; ALPHA-AMINOADIPIC SEMIALDEHYDE DEHYDROGENASE; 1.
DR PANTHER; PTHR43521:SF7; DELTA-1-PYRROLINE-5-CARBOXYLATE DEHYDROGENASE 12A1, MITOCHONDRIAL; 1.
DR Pfam; PF00171; Aldedh; 1.
DR SUPFAM; SSF53720; ALDH-like; 1.
DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000006727}.
FT DOMAIN 78..513
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
SQ SEQUENCE 571 AA; 63298 MW; 8A8775CEBE5C0850 CRC64;
MQRCVVKRVG AVYGRSRSVI GKASSECLHP SFTHRSSSTL LSDHRPQSSL SFASCDADKL
SEAHQYQMHN LVQGKWEQTS KSIELLDPLN GEKFISVPDT SIDEISPFVQ SLRACSKSGL
HNPLKNPERY LLYGDIMAKA AHLLKQPQVE TFFARLIQRV APKSFAQAVG EVTVTQKFLE
NFSGDQVRFL ARSFVVPGNY QGQQSNGMRW PYGPVAIITP FNFPLEIPAL QALGALFMGN
KPILKVDSKV SIVMEQFIRL LHKCGMPPTD MDFINSDGPV MNKLLLEAEP KTTLFTGSSK
VAEKLALDLK GRVKLEDAGF DWKILGPDVQ NEDYVAWVCD QDAYACSGQK CSAQSILFMH
ENWANQNFLE RLKKLASKRK LEDLTVGPVL TVTTERMLDH VKNLLAIPGA RVEFGGKPLT
NHTIPDVYGA LEPTAVFVPL KEILRNEENF ALATTEIFGP FQILTEYKHE DLPLVFEACE
RMHAHLTAAV VSNDVHFLQE VLSNTVNGTT YAGIRARTTG APQNHWFGPA GDPRGAGIGT
PEAIKLVWSC HREIIQDVGP IPNGWSTPQC T
//
