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Database: UniProt
Entry: A0A2S9AD19_9MICO
LinkDB: A0A2S9AD19_9MICO
Original site: A0A2S9AD19_9MICO 
ID   A0A2S9AD19_9MICO        Unreviewed;       346 AA.
AC   A0A2S9AD19;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=Alanine racemase C-terminal domain-containing protein {ECO:0000259|SMART:SM01005};
GN   ORFNames=CQ047_04340 {ECO:0000313|EMBL:PRB11469.1};
OS   Microbacterium sp. MYb72.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Microbacterium.
OX   NCBI_TaxID=1848693 {ECO:0000313|EMBL:PRB11469.1, ECO:0000313|Proteomes:UP000238041};
RN   [1] {ECO:0000313|EMBL:PRB11469.1, ECO:0000313|Proteomes:UP000238041}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MYb72 {ECO:0000313|EMBL:PRB11469.1,
RC   ECO:0000313|Proteomes:UP000238041};
RA   Zimmermann J., Obeng N., Yang W., Obeng O., Kissoyan K., Pees B.,
RA   Dirksen P., Hoppner M., Franke A., Rosenstiel P., Leippe M., Dierking K.,
RA   Kaleta C., Schulenburg H.;
RT   "Genomic, metabolic, and phenotypic characteristics of bacterial isolates
RT   from the natural microbiome of the model nematode Caenorhabditis elegans.";
RL   Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|PIRSR:PIRSR600821-50};
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:PRB11469.1}.
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DR   EMBL; PCOT01000005; PRB11469.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2S9AD19; -.
DR   OrthoDB; 9813814at2; -.
DR   Proteomes; UP000238041; Unassembled WGS sequence.
DR   GO; GO:0008784; F:alanine racemase activity; IEA:InterPro.
DR   GO; GO:0006522; P:alanine metabolic process; IEA:InterPro.
DR   Gene3D; 3.20.20.10; Alanine racemase; 1.
DR   InterPro; IPR000821; Ala_racemase.
DR   InterPro; IPR009006; Ala_racemase/Decarboxylase_C.
DR   InterPro; IPR011079; Ala_racemase_C.
DR   InterPro; IPR001608; Ala_racemase_N.
DR   InterPro; IPR020622; Ala_racemase_pyridoxalP-BS.
DR   InterPro; IPR029066; PLP-binding_barrel.
DR   PANTHER; PTHR30511; ALANINE RACEMASE; 1.
DR   PANTHER; PTHR30511:SF0; ALANINE RACEMASE, CATABOLIC-RELATED; 1.
DR   Pfam; PF00842; Ala_racemase_C; 1.
DR   Pfam; PF01168; Ala_racemase_N; 1.
DR   PRINTS; PR00992; ALARACEMASE.
DR   SMART; SM01005; Ala_racemase_C; 1.
DR   SUPFAM; SSF50621; Alanine racemase C-terminal domain-like; 1.
DR   SUPFAM; SSF51419; PLP-binding barrel; 1.
DR   PROSITE; PS00395; ALANINE_RACEMASE; 1.
PE   4: Predicted;
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR600821-50}.
FT   DOMAIN          240..345
FT                   /note="Alanine racemase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01005"
FT   MOD_RES         34
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600821-50"
SQ   SEQUENCE   346 AA;  36795 MW;  FF086E0C140D413A CRC64;
     MTRPQLRLSS ARFIANIDAV RERISPSELM LVMKDDAYGH GITWAVETAA RTSVEWFGSY
     DVRGGLEIRR ILERPARVFA WATATDDEID DALLQRIDLG VGTDEYLDRI IARAVALGLC
     ARIHLKIDTG LHRNGVLPED WAAVVERARA AEASGAIELV GVWSHLAEAS DAEDDDAQNA
     FLDAVQVVNA SGAAPEALHL TASAASWWRP ELRGSVSRIG AFCYGVRSAD GPELDGILPV
     AELTATVVEI ADGAAVIGIG SFDGLLSTLA GMPVGTESGT RLLTSIGHTT SVMSDAADLA
     VGDTVWIFGA GAHGEVSATS LAERVDTVGE EILTRLTSRV RRVVID
//
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