ID Q8PB64_XANCP Unreviewed; 501 AA.
AC Q8PB64;
DT 01-OCT-2002, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2002, sequence version 1.
DT 24-JAN-2024, entry version 117.
DE RecName: Full=methylmalonate-semialdehyde dehydrogenase (CoA acylating) {ECO:0000256|ARBA:ARBA00013048};
DE EC=1.2.1.27 {ECO:0000256|ARBA:ARBA00013048};
GN Name=mmsA {ECO:0000313|EMBL:AAM40558.1};
GN OrderedLocusNames=XCC1260 {ECO:0000313|EMBL:AAM40558.1};
OS Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB
OS 528 / LMG 568 / P 25).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=190485 {ECO:0000313|EMBL:AAM40558.1, ECO:0000313|Proteomes:UP000001010};
RN [1] {ECO:0000313|EMBL:AAM40558.1, ECO:0000313|Proteomes:UP000001010}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25
RC {ECO:0000313|Proteomes:UP000001010};
RX PubMed=12024217; DOI=10.1038/417459a;
RA da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R.,
RA Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F.Jr.,
RA Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G.,
RA Cannavan F., Cardozo J., Chambergo F., Ciapina L.P., Cicarelli R.M.B.,
RA Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B.,
RA Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F.,
RA Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T.,
RA Leite R.P.Jr., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A.,
RA Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J.,
RA Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M.,
RA Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A.Jr., Rossi A.,
RA Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A.,
RA Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M.,
RA Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.;
RT "Comparison of the genomes of two Xanthomonas pathogens with differing host
RT specificities.";
RL Nature 417:459-463(2002).
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DR EMBL; AE008922; AAM40558.1; -; Genomic_DNA.
DR RefSeq; NP_636634.1; NC_003902.1.
DR RefSeq; WP_011036454.1; NC_003902.1.
DR AlphaFoldDB; Q8PB64; -.
DR STRING; 190485.XCC1260; -.
DR EnsemblBacteria; AAM40558; AAM40558; XCC1260.
DR KEGG; xcc:XCC1260; -.
DR PATRIC; fig|190485.4.peg.1350; -.
DR eggNOG; COG1012; Bacteria.
DR HOGENOM; CLU_005391_1_10_6; -.
DR OMA; VGAAKEW; -.
DR OrthoDB; 9812625at2; -.
DR Proteomes; UP000001010; Chromosome.
DR GO; GO:0018478; F:malonate-semialdehyde dehydrogenase (acetylating) activity; IBA:GO_Central.
DR GO; GO:0004491; F:methylmalonate-semialdehyde dehydrogenase (acylating, NAD) activity; IBA:GO_Central.
DR GO; GO:0006210; P:thymine catabolic process; IBA:GO_Central.
DR GO; GO:0006574; P:valine catabolic process; IBA:GO_Central.
DR CDD; cd07085; ALDH_F6_MMSDH; 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; IPR010061; MeMal-semiAld_DH.
DR NCBIfam; TIGR01722; MMSDH; 1.
DR PANTHER; PTHR43866; MALONATE-SEMIALDEHYDE DEHYDROGENASE; 1.
DR PANTHER; PTHR43866:SF3; METHYLMALONATE-SEMIALDEHYDE DEHYDROGENASE [ACYLATING], MITOCHONDRIAL; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000001010}.
FT DOMAIN 23..480
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
SQ SEQUENCE 501 AA; 52753 MW; DD12532FC233C830 CRC64;
MSESVPRVSL LIDGALVVSA TTHWQDVVNP ADQSVLAQVP FATPAEVDAA VAAAQQAFVG
WRKTPIGTRA RIFLKYQQLI REHMPELAAI LSAEQGKTLA DAEGDVFRGL EVVEHAAAIG
NLQLGELANN VANGVDTYTL LQPLGVCAGI TPFNFPAMIP LWMFPMAIAT GNTFVLKPSE
QDPMVTMRLV ELALEAGIPK GVLNVVHGGE EVVNALCDHP DIKALSFVGS TKVGTHVYRR
ASLAGKRVQC MMGAKNHAVV LPDANQEQTL NAMVGAAFGA AGQRCMAAST LVLVGEARQW
IPALVAKARG LKLGAGSTPG TDVGPLISCA ARERVEGLIA SGVAQGATLE LDGRTPQVPG
LEHGNFVGPT IFSGVTPGMR IYDEEIFGPV LVILEAATLE EAIALVNANP NGNGTALFTQ
SGAAARRFQE DIDVGQVGIN VPIPVPVPLF SFTGSRASKL GDLGPYGKQV VMFYTQTKTI
TARWFDDETL GHGVNTTISL K
//