ID B1MJX7_MYCA9 Unreviewed; 314 AA.
AC B1MJX7;
DT 29-APR-2008, integrated into UniProtKB/TrEMBL.
DT 29-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 80.
DE SubName: Full=NAD-binding protein (D-isomer specific 2-hydroxyacid dehydrogenase?) {ECO:0000313|EMBL:CAM64484.1};
GN OrderedLocusNames=MAB_4414 {ECO:0000313|EMBL:CAM64484.1};
OS Mycobacteroides abscessus (strain ATCC 19977 / DSM 44196 / CCUG 20993 / CIP
OS 104536 / JCM 13569 / NCTC 13031 / TMC 1543 / L948) (Mycobacterium
OS abscessus).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacteroides; Mycobacteroides abscessus.
OX NCBI_TaxID=561007 {ECO:0000313|EMBL:CAM64484.1, ECO:0000313|Proteomes:UP000007137};
RN [1] {ECO:0000313|EMBL:CAM64484.1, ECO:0000313|Proteomes:UP000007137}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19977 / DSM 44196 / CIP 104536 / JCM 13569 / NCTC 13031 /
RC TMC 1543 {ECO:0000313|Proteomes:UP000007137};
RX PubMed=19543527; DOI=10.1371/journal.pone.0005660;
RA Ripoll F., Pasek S., Schenowitz C., Dossat C., Barbe V., Rottman M.,
RA Macheras E., Heym B., Herrmann J.L., Daffe M., Brosch R., Risler J.L.,
RA Gaillard J.L.;
RT "Non mycobacterial virulence genes in the genome of the emerging pathogen
RT Mycobacterium abscessus.";
RL PLoS ONE 4:E5660-E5660(2009).
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000256|RuleBase:RU003719}.
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DR EMBL; CU458896; CAM64484.1; -; Genomic_DNA.
DR RefSeq; WP_005089422.1; NZ_MLCG01000001.1.
DR AlphaFoldDB; B1MJX7; -.
DR GeneID; 66969847; -.
DR KEGG; mab:MAB_4414; -.
DR Proteomes; UP000007137; 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 CDD; cd05300; 2-Hacid_dh_1; 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; IPR006140; D-isomer_DH_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR43333; 2-HACID_DH_C DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43333:SF1; 2-HACID_DH_C DOMAIN-CONTAINING PROTEIN; 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.
PE 3: Inferred from homology;
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003719}.
FT DOMAIN 37..305
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 112..273
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 314 AA; 34287 MW; AC2C71C15AEFBD3E CRC64;
MNEQLVRRPV IAVQHSPDSV PERLAPVTAA AEVRLVESDR LATALPGAEV LFVYDFRSSA
LRETWSAADS LRWVQIASTG VDPVLFDEFV ASDVVLTNSR GIFERPIAEY VLAQILAFAK
DIRRSTRAQA ALSWRHFESE SIEGTPVGVL GTGPIGQAIS TLLGAVGMRV TVLGRAESAD
LSSHVGEFEY LVLAAPLTPQ TRGIVNARVL SAMRPTARLI NVGRGELVGT WDLVSALNRG
GIAGAALDVT DPEPLPVGHP LWRTPNTHIT PHNSGDVRGW SDRLQDQFVV NFERYLRGEE
LLNIVDKNRM HRHA
//