ID C3ZG63_BRAFL Unreviewed; 497 AA.
AC C3ZG63;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 24-JAN-2024, entry version 60.
DE RecName: Full=Aldehyde dehydrogenase domain-containing protein {ECO:0000259|Pfam:PF00171};
GN Name=2 {ECO:0000313|EMBL:EEN48538.1};
GN Synonyms=3b {ECO:0000313|EMBL:EEN48538.1}, Aldh1a1
GN {ECO:0000313|EMBL:EEN48538.1};
GN ORFNames=BRAFLDRAFT_290739 {ECO:0000313|EMBL:EEN48538.1};
OS Branchiostoma floridae (Florida lancelet) (Amphioxus).
OC Eukaryota; Metazoa; Chordata; Cephalochordata; Leptocardii; Amphioxiformes;
OC Branchiostomatidae; Branchiostoma.
OX NCBI_TaxID=7739 {ECO:0000313|EMBL:EEN48538.1};
RN [1] {ECO:0000313|EMBL:EEN48538.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN48538.1};
RC TISSUE=Testes {ECO:0000313|EMBL:EEN48538.1};
RX PubMed=18563158; DOI=10.1038/nature06967;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Putnam N.H., Butts T., Ferrier D.E.K., Furlong R.F., Hellsten U.,
RA Kawashima T., Robinson-Rechavi M., Shoguchi E., Terry A., Yu J.-K.,
RA Benito-Gutierrez E.L., Dubchak I., Garcia-Fernandez J., Gibson-Brown J.J.,
RA Grigoriev I.V., Horton A.C., de Jong P.J., Jurka J., Kapitonov V.V.,
RA Kohara Y., Kuroki Y., Lindquist E., Lucas S., Osoegawa K., Pennacchio L.A.,
RA Salamov A.A., Satou Y., Sauka-Spengler T., Schmutz J., Shin-I T.,
RA Toyoda A., Bronner-Fraser M., Fujiyama A., Holland L.Z., Holland P.W.H.,
RA Satoh N., Rokhsar D.S.;
RT "The amphioxus genome and the evolution of the chordate karyotype.";
RL Nature 453:1064-1071(2008).
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000256|RuleBase:RU003345}.
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DR EMBL; GG666616; EEN48538.1; -; Genomic_DNA.
DR RefSeq; XP_002592527.1; XM_002592481.1.
DR AlphaFoldDB; C3ZG63; -.
DR STRING; 7739.C3ZG63; -.
DR eggNOG; KOG2450; Eukaryota.
DR InParanoid; C3ZG63; -.
DR GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; IBA:GO_Central.
DR CDD; cd07141; ALDH_F1AB_F2_RALDH1; 1.
DR InterPro; IPR016161; Ald_DH/histidinol_DH.
DR InterPro; IPR016163; Ald_DH_C.
DR InterPro; IPR016160; Ald_DH_CS_CYS.
DR InterPro; IPR029510; Ald_DH_CS_GLU.
DR InterPro; IPR016162; Ald_DH_N.
DR InterPro; IPR015590; Aldehyde_DH_dom.
DR PANTHER; PTHR11699:SF211; ALDEHYDE DEHYDROGENASE FAMILY 16 MEMBER A1; 1.
DR PANTHER; PTHR11699; ALDEHYDE DEHYDROGENASE-RELATED; 1.
DR Pfam; PF00171; Aldedh; 1.
DR SUPFAM; SSF53720; ALDH-like; 1.
DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|RuleBase:RU003345}.
FT DOMAIN 26..489
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 266
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ SEQUENCE 497 AA; 54292 MW; 9BAE918E2A12A099 CRC64;
MAAPYLPTPN PNPEIKFTQL FINNEFVNSA SGKTFPTINP ATGEKICDVQ EAEKADVDKA
VAAARAAFKL GTPWRTMDAS QRGRLLYKLA DLMERDKDYL ANLETLDNGK PLFESYYVDV
LEPIKIVRYF AGWCDKITGK TIPVDGPHFT YTRHEPVGVC GQIIPWNFPI NMVVWKIAPA
LACGNTCVLK PAEQTPLTAL YLAALVKEAG FPPGVVNVLA GYGPTCGAHI VEHLDVDKVA
FTGSTEIGKI IQAGAGNSNL KRVSLELGGK SPNIIFADAD MDHAVEEAHQ ALFFNMGQCC
CAGSRTFVEE SVYDEFIKRS VERAKKRTVG SPFDPKNEQG PQIDDEQFQK ILGLIESGKT
QGAKLQCGGA RHGDKGYFIE PTVFSDVGDD MTIAKEEIFG PVQSIFKFKN MEEVIERANN
TTYGLAAAVF TKDINKALTI ANSVKAGTVW VNCYNAITPQ TPFGGFKQSG NGRELGEYAL
EEYCEVKTVT VKLPGKM
//