ID D2BFP4_STRRD Unreviewed; 488 AA.
AC D2BFP4;
DT 09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT 09-FEB-2010, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE SubName: Full=Betaine-aldehyde dehydrogenase {ECO:0000313|EMBL:ACZ90205.1};
DE EC=1.2.1.8 {ECO:0000313|EMBL:ACZ90205.1};
GN OrderedLocusNames=Sros_7524 {ECO:0000313|EMBL:ACZ90205.1};
OS Streptosporangium roseum (strain ATCC 12428 / DSM 43021 / JCM 3005 / NI
OS 9100).
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Streptosporangiaceae; Streptosporangium.
OX NCBI_TaxID=479432 {ECO:0000313|EMBL:ACZ90205.1, ECO:0000313|Proteomes:UP000002029};
RN [1] {ECO:0000313|EMBL:ACZ90205.1, ECO:0000313|Proteomes:UP000002029}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12428 / DSM 43021 / JCM 3005 / NI 9100
RC {ECO:0000313|Proteomes:UP000002029};
RX PubMed=21304675; DOI=10.4056/sigs.631049;
RA Nolan M., Sikorski J., Jando M., Lucas S., Lapidus A., Glavina Del Rio T.,
RA Chen F., Tice H., Pitluck S., Cheng J.F., Chertkov O., Sims D., Meincke L.,
RA Brettin T., Han C., Detter J.C., Bruce D., Goodwin L., Land M., Hauser L.,
RA Chang Y.J., Jeffries C.D., Ivanova N., Mavromatis K., Mikhailova N.,
RA Chen A., Palaniappan K., Chain P., Rohde M., Goker M., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Streptosporangium roseum type strain (NI
RT 9100).";
RL Stand. Genomic Sci. 2:29-37(2010).
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000256|RuleBase:RU003345}.
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DR EMBL; CP001814; ACZ90205.1; -; Genomic_DNA.
DR RefSeq; WP_012893935.1; NC_013595.1.
DR AlphaFoldDB; D2BFP4; -.
DR STRING; 479432.Sros_7524; -.
DR KEGG; sro:Sros_7524; -.
DR eggNOG; COG1012; Bacteria.
DR HOGENOM; CLU_005391_0_1_11; -.
DR OrthoDB; 3802174at2; -.
DR Proteomes; UP000002029; Chromosome.
DR GO; GO:0018480; F:5-carboxymethyl-2-hydroxymuconic-semialdehyde dehydrogenase activity; IEA:InterPro.
DR GO; GO:0008802; F:betaine-aldehyde dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:1901023; P:4-hydroxyphenylacetate catabolic process; IEA:InterPro.
DR CDD; cd07093; ALDH_F8_HMSADH; 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 InterPro; IPR011985; DH_HpaE.
DR NCBIfam; TIGR02299; HpaE; 1.
DR PANTHER; PTHR43720; 2-AMINOMUCONIC SEMIALDEHYDE DEHYDROGENASE; 1.
DR PANTHER; PTHR43720:SF2; 2-AMINOMUCONIC SEMIALDEHYDE DEHYDROGENASE; 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|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003345};
KW Reference proteome {ECO:0000313|Proteomes:UP000002029}.
FT DOMAIN 15..472
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 248
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ SEQUENCE 488 AA; 52204 MW; 9BBCED820D8667D5 CRC64;
MNLEHYIGGA HVPSVSGATF DALEPASNET YLTVAAGGPE DIAAAVAAAR KAFTDGPWPR
MTGEQRATVL RRIAAAIESR DDRIAALECR DTGLPITQAR GQAHRAAHNF RFFADVITTL
GEDVYRVASA QLNYVLRKPV GVAGLITPWN TPFMLETWKL APALAAGCPV VLKPAEWSPA
SAGLLPEIME EAGLPAGVFN LVHGIGEEAG AALVEHPDVP VISFTGETGT GQVIMRTAAA
NLKTLSMELG GKSPLIVFDD ADLDRALDAA VFGVFSLNGE RCTASSRVLV QDTVYESFVA
RLAERASRVR VGSPDDPATE LGALVHPEHY ERVMDYVRIG VEEGARLVAG GSRPADLPVG
NFLSATVFAD VTPNMRIFQE EIFGPVVCVT PFSTEAEALE LANATRYGLA AYLWTNDLRR
THRLAQSVEA GMLWVNSQNV RDLRTPFGGV KASGLGREGG RHSIDVYTES HIVHLATEDM
PIPRFGAA
//
