ID   A0M6P9_CHRFK            Unreviewed;       369 AA.
AC   A0M6P9;
DT   12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT   12-DEC-2006, sequence version 1.
DT   27-MAR-2024, entry version 108.
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:CAL68294.1};
GN   OrderedLocusNames=GFO_3353 {ECO:0000313|EMBL:CAL68294.1};
OS   Christiangramia forsetii (strain DSM 17595 / CGMCC 1.15422 / KT0803)
OS   (Gramella forsetii).
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Christiangramia.
OX   NCBI_TaxID=411154 {ECO:0000313|EMBL:CAL68294.1, ECO:0000313|Proteomes:UP000000755};
RN   [1] {ECO:0000313|EMBL:CAL68294.1, ECO:0000313|Proteomes:UP000000755}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KT0803 {ECO:0000313|EMBL:CAL68294.1,
RC   ECO:0000313|Proteomes:UP000000755};
RX   PubMed=17107561; DOI=10.1111/j.1462-2920.2006.01152.x;
RA   Bauer M., Kube M., Teeling H., Richter M., Lombardot T., Allers E.,
RA   Wuerdemann C.A., Quast C., Kuhl H., Knaust F., Woebken D., Bischof K.,
RA   Mussmann M., Choudhuri J.V., Meyer F., Reinhardt R., Amann R.I.,
RA   Gloeckner F.O.;
RT   "Whole genome analysis of the marine Bacteroidetes'Gramella forsetii'
RT   reveals adaptations to degradation of polymeric organic matter.";
RL   Environ. Microbiol. 8:2201-2213(2006).
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; CU207366; CAL68294.1; -; Genomic_DNA.
DR   RefSeq; WP_011711195.1; NC_008571.1.
DR   AlphaFoldDB; A0M6P9; -.
DR   STRING; 411154.GFO_3353; -.
DR   KEGG; gfo:GFO_3353; -.
DR   eggNOG; COG0787; Bacteria.
DR   HOGENOM; CLU_028393_2_2_10; -.
DR   OrthoDB; 9801978at2; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000000755; 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; 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   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          243..367
FT                   /note="Alanine racemase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01005"
FT   ACT_SITE        38
FT                   /note="Proton acceptor; specific for D-alanine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT   ACT_SITE        264
FT                   /note="Proton acceptor; specific for L-alanine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT   BINDING         136
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT                   ECO:0000256|PIRSR:PIRSR600821-52"
FT   BINDING         313
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT                   ECO:0000256|PIRSR:PIRSR600821-52"
FT   MOD_RES         38
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT                   ECO:0000256|PIRSR:PIRSR600821-50"
SQ   SEQUENCE   369 AA;  41435 MW;  487B9400E2E95535 CRC64;
     MPEAKETVLE INLGNLAHNY RFLRSKTDKE AKFLSVVKAH AYGSDSVEIA KKLEELGTDY
     FAVAYVEEGI RLRENGISKP ILVLHPQPSH FEEIIEHCLE PNLYSQKTLE SFVSLAERLN
     QKNYPVHIKL NTGLNRLGFD QSEIPRVFET IKNTNSIKIA SVFSHLAASE DWQEREFTLS
     QIDLFRKMTW QLIENLDYEP LLHICNTSGV INYPKAAFSM VRTGIGLYGY SNDKTIDPHL
     KPVGKLKTII SQIRKLDPGA SVGYNRAFKT EKESKIATLP IGHADGINRI YGKQKAGVFV
     NGKYAPIVGN VCMDIIMIDV TGIDCEEGDE VIIFGGPQHP VDFARAGGTI SYELITGIQR
     RVTRKIIPE
//