ID B9EC00_MACCJ Unreviewed; 360 AA.
AC B9EC00;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 87.
DE SubName: Full=Alanine racemase 2 {ECO:0000313|EMBL:BAH17761.1};
GN Name=alr2 {ECO:0000313|EMBL:BAH17761.1};
GN OrderedLocusNames=MCCL_1054 {ECO:0000313|EMBL:BAH17761.1};
OS Macrococcus caseolyticus (strain JCSC5402).
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae; Macrococcus.
OX NCBI_TaxID=458233 {ECO:0000313|EMBL:BAH17761.1, ECO:0000313|Proteomes:UP000001383};
RN [1] {ECO:0000313|EMBL:BAH17761.1, ECO:0000313|Proteomes:UP000001383}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCSC5402 {ECO:0000313|EMBL:BAH17761.1,
RC ECO:0000313|Proteomes:UP000001383};
RX PubMed=19074389; DOI=10.1128/JB.01058-08;
RA Baba T., Kuwahara-Arai K., Uchiyama I., Takeuchi F., Ito T., Hiramatsu K.;
RT "Complete genome sequence of Macrococcus caseolyticus strain JCSCS5402,
RT reflecting the ancestral genome of the human-pathogenic staphylococci.";
RL J. Bacteriol. 191:1180-1190(2009).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|PIRSR:PIRSR600821-50};
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DR EMBL; AP009484; BAH17761.1; -; Genomic_DNA.
DR RefSeq; WP_012656959.1; NC_011999.1.
DR AlphaFoldDB; B9EC00; -.
DR STRING; 458233.MCCL_1054; -.
DR KEGG; mcl:MCCL_1054; -.
DR eggNOG; COG0787; Bacteria.
DR HOGENOM; CLU_028393_2_2_9; -.
DR OrthoDB; 9813814at2; -.
DR Proteomes; UP000001383; Chromosome.
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; IPR029066; PLP-binding_barrel.
DR NCBIfam; TIGR00492; alr; 1.
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.
PE 4: Predicted;
KW Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR600821-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000001383}.
FT DOMAIN 233..354
FT /note="Alanine racemase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01005"
FT BINDING 122
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR600821-52"
FT BINDING 300
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR600821-52"
FT MOD_RES 30
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR600821-50"
SQ SEQUENCE 360 AA; 41521 MW; BDFC5318A21A8E76 CRC64;
MTARWTVDRT KFIENVKSVI DNTPVMAVVK NNAYHYGLEF AIDAFLQAGI TTFSTTNLNE
AILIRKIAPE ATIFLMNPVT RFNDLRQYNI QMTLPSLAFY HRYQSELDGI SVHLEYENLL
HRSGFKTFEE MKTVIDDNNQ LPVHLQMNIN GIWTHFGYAD EFDVIEYEIE KESWLKGLKW
ISRYHTFEMI HSQNSASFIR DKIFDEHTHV RIGIILYGSR PYASLDESVT HQSLTVSANV
IQVRNISKGE SAGYSFAFTA EKETKLAVVD IGYGDGILRT RSKHDCIIKG RRYPIRALMM
SHMFVEVDNT VEAEDEVILY SDEIRIDEFT FKGIGANSEQ LSALNHQSLI KEYINDINIY
//
