ID H8IS45_MYCIA Unreviewed; 359 AA.
AC H8IS45;
DT 16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2012, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=Putative D-3-phosphoglycerate dehydrogenase (PGDH) {ECO:0000313|EMBL:AFC43173.1};
GN OrderedLocusNames=OCU_19540 {ECO:0000313|EMBL:AFC43173.1};
OS Mycobacterium intracellulare (strain ATCC 13950 / DSM 43223 / JCM 6384 /
OS NCTC 13025 / 3600).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium avium complex (MAC).
OX NCBI_TaxID=487521 {ECO:0000313|EMBL:AFC43173.1, ECO:0000313|Proteomes:UP000008004};
RN [1] {ECO:0000313|EMBL:AFC43173.1, ECO:0000313|Proteomes:UP000008004}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13950 / DSM 43223 / JCM 6384 / NCTC 13025 / 3600
RC {ECO:0000313|Proteomes:UP000008004};
RX PubMed=22535933; DOI=10.1128/JB.00295-12;
RA Kim B.J., Choi B.S., Lim J.S., Choi I.Y., Lee J.H., Chun J., Kook Y.H.,
RA Kim B.J.;
RT "Complete genome sequence of Mycobacterium intracellulare strain ATCC
RT 13950T.";
RL J. Bacteriol. 194:2750-2750(2012).
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00005854,
CC ECO:0000256|RuleBase:RU003719}.
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DR EMBL; CP003322; AFC43173.1; -; Genomic_DNA.
DR RefSeq; WP_008255445.1; NZ_ABIN01000266.1.
DR AlphaFoldDB; H8IS45; -.
DR GeneID; 77302511; -.
DR KEGG; mia:OCU_19540; -.
DR PATRIC; fig|487521.10.peg.1964; -.
DR eggNOG; COG1052; Bacteria.
DR HOGENOM; CLU_019796_1_3_11; -.
DR Proteomes; UP000008004; Chromosome.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0008652; P:amino acid biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd12173; PGDH_4; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR InterPro; IPR006139; D-isomer_2_OHA_DH_cat_dom.
DR InterPro; IPR029752; D-isomer_DH_CS1.
DR InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR42789; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_6G10090); 1.
DR PANTHER; PTHR42789:SF1; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_6G10090); 1.
DR Pfam; PF00389; 2-Hacid_dh; 1.
DR Pfam; PF02826; 2-Hacid_dh_C; 1.
DR SUPFAM; SSF52283; Formate/glycerate dehydrogenase catalytic domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00065; D_2_HYDROXYACID_DH_1; 1.
PE 3: Inferred from homology;
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003719}.
FT DOMAIN 73..331
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 123..299
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 359 AA; 37988 MW; A5BB718A93FFD263 CRC64;
MTGAPRPRLV VERWTDPAAA DVLELSGIDI VKLDLTAPAE SGWAALESAH GYQVATRTDV
ASVADGAQWL AGEALIARCP CLLAVCSAGA GYDVIDVDAC TRAGIAVCNN SGPGAEAVAE
HALGFMLDLA KKITVSDRAL RSGPLRDRLA LRGTQLFGKT LGVVGLGAIG GRLVELCAPF
GMEVLVFDPY LDETTARSRG VQQVTLAELV ERSDFVQVTC PLTSETRGLI GRTQFAAMKP
TAFFITTARG PVHDEAALLD ALVSGGIAGA GLDVFHEEPP RQDNPLLQLD NVVATPHTAG
ITVEAARDIA VATATQWQTI FEGRMPPRLL NPQVWPRYCE RFHDILGVHP TARVPAAAE
//
