ID C6XSA9_PEDHD Unreviewed; 454 AA.
AC C6XSA9;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE SubName: Full=Aldehyde Dehydrogenase {ECO:0000313|EMBL:ACU03454.1};
GN OrderedLocusNames=Phep_1238 {ECO:0000313|EMBL:ACU03454.1};
OS Pedobacter heparinus (strain ATCC 13125 / DSM 2366 / CIP 104194 / JCM 7457
OS / NBRC 12017 / NCIMB 9290 / NRRL B-14731 / HIM 762-3).
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Pedobacter.
OX NCBI_TaxID=485917 {ECO:0000313|EMBL:ACU03454.1, ECO:0000313|Proteomes:UP000000852};
RN [1] {ECO:0000313|EMBL:ACU03454.1, ECO:0000313|Proteomes:UP000000852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13125 / DSM 2366 / CIP 104194 / JCM 7457 / NBRC 12017 /
RC NCIMB 9290 / NRRL B-14731 / HIM 762-3
RC {ECO:0000313|Proteomes:UP000000852};
RX PubMed=21304637; DOI=10.4056/sigs.22138;
RA Han C., Spring S., Lapidus A., Del Rio T.G., Tice H., Copeland A.,
RA Cheng J.F., Lucas S., Chen F., Nolan M., Bruce D., Goodwin L., Pitluck S.,
RA Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K.,
RA Land M., Hauser L., Chang Y.J., Jeffries C.C., Saunders E., Chertkov O.,
RA Brettin T., Goker M., Rohde M., Bristow J., Eisen J.A., Markowitz V.,
RA Hugenholtz P., Kyrpides N.C., Klenk H.P., Detter J.C.;
RT "Complete genome sequence of Pedobacter heparinus type strain (HIM 762-
RT 3).";
RL Stand. Genomic Sci. 1:54-62(2009).
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000256|RuleBase:RU003345}.
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DR EMBL; CP001681; ACU03454.1; -; Genomic_DNA.
DR RefSeq; WP_012781398.1; NZ_AQGK01000001.1.
DR AlphaFoldDB; C6XSA9; -.
DR STRING; 485917.Phep_1238; -.
DR KEGG; phe:Phep_1238; -.
DR eggNOG; COG1012; Bacteria.
DR HOGENOM; CLU_005391_1_0_10; -.
DR OrthoDB; 781568at2; -.
DR Proteomes; UP000000852; Chromosome.
DR GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR InterPro; IPR016161; Ald_DH/histidinol_DH.
DR InterPro; IPR016163; Ald_DH_C.
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; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003345};
KW Reference proteome {ECO:0000313|Proteomes:UP000000852}.
FT DOMAIN 2..448
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 226
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ SEQUENCE 454 AA; 50477 MW; D1B1B2041683D9D6 CRC64;
MNIVNPATEE IIASVKEDDS KSLAHKRNLL KVGQKNWAAR SLAERLRIIT QFYNLLDAEK
ERLAAMLTSE VGKPLQQSRN EINGAGTRIK WMLDHGAKYL SDELVTDTPE LKEYISYNPL
GIVCNISAWN YPYLVGVNVF IPALMAGNAV LYKPSEYATL TGLEIEKLLR QAGVPDDVFK
VAIGAKETGE HLLDMNFDGY FFTGSYRTGK HIYERVAPKM VPCQLELGGK DPLYVAGDVK
DVAAVAVATA DGAFYNNGQS CCSVERIYVH EKVYDDYLAA FVKEVESWKT GLPDEEGVYI
GALTRKEQLK VLELQVKDAL QYGAVLLSGG KRKGEKGNYF EPTVLTNVTN QMKVMQEESF
GPIIGIMKVN DDAEALYLMQ DTAYGLTASV YSDSWERAEN ILSQIDSGTG YWNCCDRVSA
ALPWSGRRHS GIGATLSHQG IRAFTRPRAW HLKR
//
