ID Q1YF77_AURMS Unreviewed; 499 AA.
AC Q1YF77;
DT 02-MAY-2006, integrated into UniProtKB/TrEMBL.
DT 02-MAY-2006, sequence version 1.
DT 24-JAN-2024, entry version 75.
DE RecName: Full=methylmalonate-semialdehyde dehydrogenase (CoA acylating) {ECO:0000256|ARBA:ARBA00013048};
DE EC=1.2.1.27 {ECO:0000256|ARBA:ARBA00013048};
GN ORFNames=SI859A1_03304 {ECO:0000313|EMBL:EAS49096.1};
OS Aurantimonas manganoxydans (strain ATCC BAA-1229 / DSM 21871 / SI85-9A1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Aurantimonadaceae; Aurantimonas.
OX NCBI_TaxID=287752 {ECO:0000313|EMBL:EAS49096.1, ECO:0000313|Proteomes:UP000000321};
RN [1] {ECO:0000313|EMBL:EAS49096.1, ECO:0000313|Proteomes:UP000000321}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SI85-9A1 {ECO:0000313|EMBL:EAS49096.1,
RC ECO:0000313|Proteomes:UP000000321};
RX PubMed=18344346; DOI=10.1128/AEM.01656-07;
RA Dick G.J., Podell S., Johnson H.A., Rivera-Espinoza Y., Bernier-Latmani R.,
RA McCarthy J.K., Torpey J.W., Clement B.G., Gaasterland T., Tebo B.M.;
RT "Genomic insights into Mn(II) oxidation by the marine alphaproteobacterium
RT Aurantimonas sp. strain SI85-9A1.";
RL Appl. Environ. Microbiol. 74:2646-2658(2008).
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:EAS49096.1}.
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; AAPJ01000006; EAS49096.1; -; Genomic_DNA.
DR RefSeq; WP_009211117.1; NZ_CH672387.1.
DR AlphaFoldDB; Q1YF77; -.
DR HOGENOM; CLU_005391_1_10_5; -.
DR OrthoDB; 9812625at2; -.
DR BioCyc; AURANTIMONAS:SI859A1_03304-MONOMER; -.
DR Proteomes; UP000000321; Unassembled WGS sequence.
DR GO; GO:0004491; F:methylmalonate-semialdehyde dehydrogenase (acylating, NAD) activity; IEA:UniProtKB-EC.
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: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,
KW ECO:0000313|EMBL:EAS49096.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000321}.
FT DOMAIN 16..479
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
SQ SEQUENCE 499 AA; 53336 MW; 7A0D5EFC151FDFF3 CRC64;
MEQIGHFIGG KRVAGTSGRT ADVFNPATGE VQAQVALASA DELTAAVANA KAAQPAWAAT
NPQRRARVMM KFVELLNRDM DKLAEVLSRE HGKTIPDAKG DVQRGLEVAE FCIGAPHLLK
GEFSEGAGPG IDLYSIRQAL GVVAGITPFN FPAMIPMWKF APAIAAGNAF ILKPSERDPS
VPLMLAELMI EAGLPEGILN VVNGDKGAVD AILDDPDIQA IGFVGSTPIA QYIYSRGCAN
GKRVQCFGGA KNHMIIMPDA DIDKAADALI GAGYGAAGER CMAVSVAVPV GKETADRLME
KLIPRVEALK IAPYTAGDDV DMGPLVTREA QQRVLGLIDR GVEEGAKLAV DGRGFKMQGY
ENGFFVGACL FDDVTKDMDI YKTEIFGPVL SVVRAKDYEE AIDLPMSHEY GNGVSIYTRD
GDAARDFASR INIGMVGVNV PIPVPLAYYT FGGWKASGFG DLNQHGPDAF RFYTRTKTVT
SRWPSGIKDG AEFAMPVMR
//
