ID A0A0A6VMN5_9MICC Unreviewed; 503 AA.
AC A0A0A6VMN5;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=Aldehyde dehydrogenase {ECO:0000256|PIRNR:PIRNR036492};
GN ORFNames=GY22_15835 {ECO:0000313|EMBL:KHD96365.1};
OS Kocuria polaris.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Kocuria.
OX NCBI_TaxID=136273 {ECO:0000313|EMBL:KHD96365.1, ECO:0000313|Proteomes:UP000030466};
RN [1] {ECO:0000313|EMBL:KHD96365.1, ECO:0000313|Proteomes:UP000030466}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CMS 76or {ECO:0000313|EMBL:KHD96365.1,
RC ECO:0000313|Proteomes:UP000030466};
RX PubMed=12656171; DOI=10.1099/ijs.0.02336-0;
RA Reddy G.S., Prakash J.S., Prabahar V., Matsumoto G.I., Stackebrandt E.,
RA Shivaji S.;
RT "Kocuria polaris sp. nov., an orange-pigmented psychrophilic bacterium
RT isolated from an Antarctic cyanobacterial mat sample.";
RL Int. J. Syst. Evol. Microbiol. 53:183-187(2003).
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00009986, ECO:0000256|PIRNR:PIRNR036492,
CC ECO:0000256|RuleBase:RU003345}.
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:KHD96365.1}.
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DR EMBL; JSUH01000018; KHD96365.1; -; Genomic_DNA.
DR RefSeq; WP_035929995.1; NZ_JSUH01000018.1.
DR AlphaFoldDB; A0A0A6VMN5; -.
DR OrthoDB; 6882680at2; -.
DR Proteomes; UP000030466; Unassembled WGS sequence.
DR GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0006081; P:cellular aldehyde metabolic process; IEA:InterPro.
DR CDD; cd07087; ALDH_F3-13-14_CALDH-like; 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; IPR012394; Aldehyde_DH_NAD(P).
DR PANTHER; PTHR43570; ALDEHYDE DEHYDROGENASE; 1.
DR PANTHER; PTHR43570:SF16; ALDEHYDE DEHYDROGENASE TYPE III, ISOFORM Q; 1.
DR Pfam; PF00171; Aldedh; 1.
DR PIRSF; PIRSF036492; ALDH; 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|PIRNR:PIRNR036492}.
FT DOMAIN 34..457
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 238
FT /evidence="ECO:0000256|PIRSR:PIRSR036492-1,
FT ECO:0000256|PROSITE-ProRule:PRU10007"
FT ACT_SITE 272
FT /evidence="ECO:0000256|PIRSR:PIRSR036492-1"
SQ SEQUENCE 503 AA; 53925 MW; F6859BE34C41512C CRC64;
MTSTRSTLPA PAPADDSADV PADPSADFPA DFPAVDAAVA GARAAFVPDV DLATRLDRLH
RLEDLVRENR TVLEEALATD LGKPPAEAWL TELGFTLEEI AGIRKELGRW MTPARVPVPL
SLAPARSRVE HQPLGTVLVM APWNYPVQLV LSPLAGALAA GNTVVVKPSE VSATVSGVLA
ELLERYLGDC VRVVEGGVPE TTRLLEHRFD HVFYTGNGTV ARIVMAAAAR HLTPVTLELG
GKSPVWVDGS TDLRTAARRI VWGKFLNAGQ TCVAPDHVLG TPETLAALEP ELLRAVEEHY
GEDPARSDSY GRIVTGRHLD RLVGLLEQVP AHDVVCGGTA EPGERYLAPT VVRSAPDGPL
MAEELFGPVL PLVPVASAEH AVELITAGDK PLALYVFSEE RSVKELFRRR TSSGGLSFNA
PLLHLTSPEL PFGGVGESGT GAYHGKFSFT TFSHARAVLD KPLAPDTLRV VYPPYRGLRA
RLAAAAVGLR RPRRRTRHAV SEN
//
