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Database: UniProt
Entry: I9L3Z3_LACPE
LinkDB: I9L3Z3_LACPE
Original site: I9L3Z3_LACPE 
ID   I9L3Z3_LACPE            Unreviewed;       375 AA.
AC   I9L3Z3;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   24-JAN-2024, entry version 63.
DE   RecName: Full=Alanine racemase {ECO:0000256|HAMAP-Rule:MF_01201};
DE            EC=5.1.1.1 {ECO:0000256|HAMAP-Rule:MF_01201};
GN   Name=alr {ECO:0000313|EMBL:EIW14921.1};
GN   ORFNames=KCA1_0432 {ECO:0000313|EMBL:EIW14921.1};
OS   Lactiplantibacillus pentosus KCA1.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactiplantibacillus.
OX   NCBI_TaxID=1136177 {ECO:0000313|EMBL:EIW14921.1};
RN   [1] {ECO:0000313|EMBL:EIW14921.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KCA1 {ECO:0000313|EMBL:EIW14921.1};
RX   PubMed=23527145;
RA   Anukam K.C., Macklaim J.M., Gloor G.B., Reid G., Boekhorst J., Renckens B.,
RA   van Hijum S.A., Siezen R.J.;
RT   "Genome Sequence of Lactobacillus pentosus KCA1: Vaginal Isolate from a
RT   Healthy Premenopausal Woman.";
RL   PLoS ONE 8:E59239-E59239(2013).
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,
CC         ECO:0000256|HAMAP-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}.
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:EIW14921.1}.
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DR   EMBL; AKAO01000012; EIW14921.1; -; Genomic_DNA.
DR   RefSeq; WP_003637680.1; NZ_CM001538.1.
DR   AlphaFoldDB; I9L3Z3; -.
DR   PATRIC; fig|1136177.4.peg.19; -.
DR   eggNOG; COG0787; Bacteria.
DR   HOGENOM; CLU_028393_2_1_9; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000005826; 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}.
FT   DOMAIN          249..374
FT                   /note="Alanine racemase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01005"
FT   ACT_SITE        41
FT                   /note="Proton acceptor; specific for D-alanine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT   ACT_SITE        270
FT                   /note="Proton acceptor; specific for L-alanine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT   BINDING         141
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT                   ECO:0000256|PIRSR:PIRSR600821-52"
FT   BINDING         317
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT                   ECO:0000256|PIRSR:PIRSR600821-52"
FT   MOD_RES         41
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT                   ECO:0000256|PIRSR:PIRSR600821-50"
SQ   SEQUENCE   375 AA;  40555 MW;  F9FC7EF852B7C25D CRC64;
     MVVIGEHRHT QVTVDLQAIK TNISAEMAQK DELTELWAVV KANGYGHGII QVAQAAKEAG
     ATGFCVAILD EALALRAAGL TEPILVLGIT EPEFAPLAAE KDISLAVGTQ AWLKTAAAIL
     TANEVVTPLH VHLALDTGMG RIGFQTPGEL AQAVAVLRQP KSPFDFEGIF THFATADQAD
     DTYFTHQLNQ WKKLIAAVDE LPKYVHVSNS ATSLWHQACN GNMVRFGVAL YGLNPSGREL
     STPYPLQPAL SLTAQLTFVK RLARGKSVSY GATYTADQDE WIGTVPIGYA DGYERRLQGF
     HVLVDGEFCE IVGRVCMDQL MVRLPHEVPV GAKVTLVGTD GDNTITLQDI ADYCGTIHYE
     IACGLATRVP RVYVD
//
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