ID F3GIG4_PSESJ Unreviewed; 339 AA.
AC F3GIG4;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 24-JAN-2024, entry version 54.
DE RecName: Full=methylmalonate-semialdehyde dehydrogenase (CoA acylating) {ECO:0000256|ARBA:ARBA00013048};
DE EC=1.2.1.27 {ECO:0000256|ARBA:ARBA00013048};
DE Flags: Fragment;
GN ORFNames=PSYPI_33073 {ECO:0000313|EMBL:EGH46867.1};
OS Pseudomonas syringae pv. pisi str. 1704B.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX NCBI_TaxID=629263 {ECO:0000313|EMBL:EGH46867.1, ECO:0000313|Proteomes:UP000004986};
RN [1] {ECO:0000313|EMBL:EGH46867.1, ECO:0000313|Proteomes:UP000004986}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1704B {ECO:0000313|EMBL:EGH46867.1,
RC ECO:0000313|Proteomes:UP000004986};
RX PubMed=21799664; DOI=10.1371/journal.ppat.1002132;
RA Baltrus D.A., Nishimura M.T., Romanchuk A., Chang J.H., Mukhtar M.S.,
RA Cherkis K., Roach J., Grant S.R., Jones C.D., Dangl J.L.;
RT "Dynamic evolution of pathogenicity revealed by sequencing and comparative
RT genomics of 19 Pseudomonas syringae isolates.";
RL PLoS Pathog. 7:E1002132-e1002132(2011).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EGH46867.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AEAI01001824; EGH46867.1; -; Genomic_DNA.
DR AlphaFoldDB; F3GIG4; -.
DR PATRIC; fig|629263.4.peg.5252; -.
DR HOGENOM; CLU_005391_1_10_6; -.
DR BioCyc; PSYR629263:G11X0-6002-MONOMER; -.
DR Proteomes; UP000004986; Unassembled WGS sequence.
DR GO; GO:0004491; F:methylmalonate-semialdehyde dehydrogenase (acylating, NAD) activity; IEA:InterPro.
DR GO; GO:0071704; P:organic substance metabolic process; IEA:UniProt.
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; IPR010061; MeMal-semiAld_DH.
DR NCBIfam; TIGR01722; MMSDH; 1.
DR PANTHER; PTHR43866; MALONATE-SEMIALDEHYDE DEHYDROGENASE; 1.
DR PANTHER; PTHR43866:SF4; MALONATE-SEMIALDEHYDE DEHYDROGENASE; 1.
DR Pfam; PF00171; Aldedh; 1.
DR SUPFAM; SSF53720; ALDH-like; 1.
DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 3..319
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EGH46867.1"
SQ SEQUENCE 339 AA; 36262 MW; C7497600658F2DA2 CRC64;
YPLAIACGNC FILKPSERDP SSTLLIAELL HEAGLPKGVL NVVHGDKVAV DALIEAPEVK
ALSFVGSTPI AEYIYKEGAA RGKRVQALGG AKNHAVLMPD ADLDNAVSAL MGAAYGSCGE
RCMAISVAVC VGDQIADALV AKLVPQIQSL KIGAGTTCGL DMGPLVTGQH RDKVGGYIED
GVQAGATLVV DGRNLQVAGH EQGFFMGGCL FDRVTPEMRI YKEEIFGPVL CIVRVDSLEQ
AMQLINDHEY GNGTCIFTRD GEAARLFCDE IEVGMVGVNV PLPVPVAYHS FGGWKRSLFG
DLHAYGPDGV RFYTRRKAIT QRWPQRASHE ASQFAFPSL
//