ID   C7R176_JONDD            Unreviewed;       410 AA.
AC   C7R176;
DT   13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT   13-OCT-2009, sequence version 1.
DT   27-MAR-2024, entry version 86.
DE   RecName: Full=Alanine racemase {ECO:0000256|HAMAP-Rule:MF_01201};
DE            EC=5.1.1.1 {ECO:0000256|HAMAP-Rule:MF_01201};
GN   OrderedLocusNames=Jden_0627 {ECO:0000313|EMBL:ACV08291.1};
OS   Jonesia denitrificans (strain ATCC 14870 / DSM 20603 / BCRC 15368 / CIP
OS   55.134 / JCM 11481 / NBRC 15587 / NCTC 10816 / Prevot 55134) (Listeria
OS   denitrificans).
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Jonesiaceae;
OC   Jonesia.
OX   NCBI_TaxID=471856 {ECO:0000313|EMBL:ACV08291.1, ECO:0000313|Proteomes:UP000000628};
RN   [1] {ECO:0000313|EMBL:ACV08291.1, ECO:0000313|Proteomes:UP000000628}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14870 / DSM 20603 / BCRC 15368 / CIP 55.134 / JCM 11481 /
RC   NBRC 15587 / NCTC 10816 / Prevot 55134
RC   {ECO:0000313|Proteomes:UP000000628};
RX   PubMed=21304666; DOI=10.4056/sigs.41646;
RA   Pukall R., Gehrich-Schroter G., Lapidus A., Nolan M., Glavina Del Rio T.,
RA   Lucas S., Chen F., Tice H., Pitluck S., Cheng J.F., Copeland A.,
RA   Saunders E., Brettin T., Detter J.C., Bruce D., Goodwin L., Pati A.,
RA   Ivanova N., Mavromatis K., Ovchinnikova G., Chen A., Palaniappan K.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Chain P., Goker M.,
RA   Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C.,
RA   Klenk H.P., Han C.;
RT   "Complete genome sequence of Jonesia denitrificans type strain (Prevot
RT   55134).";
RL   Stand. Genomic Sci. 1:262-269(2009).
CC   -!- FUNCTION: Catalyzes the interconversion of L-alanine and D-alanine. May
CC       also act on other amino acids. {ECO:0000256|HAMAP-Rule:MF_01201}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-alanine = D-alanine; Xref=Rhea:RHEA:20249,
CC         ChEBI:CHEBI:57416, ChEBI:CHEBI:57972; EC=5.1.1.1;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01201};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933, ECO:0000256|HAMAP-
CC         Rule:MF_01201, ECO:0000256|PIRSR:PIRSR600821-50};
CC   -!- PATHWAY: Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine
CC       from L-alanine: step 1/1. {ECO:0000256|HAMAP-Rule:MF_01201}.
CC   -!- SIMILARITY: Belongs to the alanine racemase family. {ECO:0000256|HAMAP-
CC       Rule:MF_01201}.
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DR   EMBL; CP001706; ACV08291.1; -; Genomic_DNA.
DR   RefSeq; WP_015770919.1; NC_013174.1.
DR   AlphaFoldDB; C7R176; -.
DR   STRING; 471856.Jden_0627; -.
DR   KEGG; jde:Jden_0627; -.
DR   eggNOG; COG0787; Bacteria.
DR   HOGENOM; CLU_028393_0_0_11; -.
DR   OrthoDB; 9813814at2; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000000628; Chromosome.
DR   GO; GO:0008784; F:alanine racemase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0030632; P:D-alanine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd00430; PLPDE_III_AR; 1.
DR   Gene3D; 3.20.20.10; Alanine racemase; 1.
DR   HAMAP; MF_01201; Ala_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   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.
DR   PROSITE; PS00395; ALANINE_RACEMASE; 1.
PE   3: Inferred from homology;
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_01201};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, ECO:0000256|HAMAP-
KW   Rule:MF_01201}; Reference proteome {ECO:0000313|Proteomes:UP000000628}.
FT   DOMAIN          259..391
FT                   /note="Alanine racemase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01005"
FT   ACT_SITE        48
FT                   /note="Proton acceptor; specific for D-alanine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT   ACT_SITE        280
FT                   /note="Proton acceptor; specific for L-alanine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT   BINDING         146
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT                   ECO:0000256|PIRSR:PIRSR600821-52"
FT   BINDING         333
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT                   ECO:0000256|PIRSR:PIRSR600821-52"
FT   MOD_RES         48
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT                   ECO:0000256|PIRSR:PIRSR600821-50"
SQ   SEQUENCE   410 AA;  42844 MW;  8F8F7BAA0CDC0FDF CRC64;
     MSDNHQPPPG TYPGRAIIDL AAISQNVSTL ATRLGDNGSH AAIMAVVKAN AYGHGLVPAA
     RAALHGGATW LGVAHAHEAL ALRQAGITDR ILTWLHAPGV PYRDLIAADI DVSVAAPWAA
     QEVISAAQAA GRPARVHLKV DTGLGRNGVT PADLPFLLAT LIDAQHAGHL TLVGVWSHLA
     FADEPHHPSV REQARVFDDA ITIVQAAGAH LEVRHIANSA ATLTAPELAY DLVRPGLAIY
     GLSPIPQVAS AAELGLRPAM TVQADIATAK RLPAGHGVSY AHHYVTARDT HIAVIPLGYA
     DGIPRHASGH NGELGAPVSI NGVTYAIAGR VCMDQIVIDV HDDSVRAGHT ATLFGDPTLG
     VPSAQQWADA TGTISYEITT RIADRLPRMY LPTSDLHHAP TVSQHSHTGG
//