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Database: UniProt/TrEMBL
Entry: C6XHR3_LIBAP
LinkDB: C6XHR3_LIBAP
Original site: C6XHR3_LIBAP 
ID   C6XHR3_LIBAP            Unreviewed;       370 AA.
AC   C6XHR3;
DT   22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   22-SEP-2009, sequence version 1.
DT   27-SEP-2017, entry version 67.
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=CLIBASIA_01090 {ECO:0000313|EMBL:ACT56806.1};
OS   Liberibacter asiaticus (strain psy62).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Liberibacter.
OX   NCBI_TaxID=537021 {ECO:0000313|EMBL:ACT56806.1, ECO:0000313|Proteomes:UP000002744};
RN   [1] {ECO:0000313|EMBL:ACT56806.1, ECO:0000313|Proteomes:UP000002744}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=psy62 {ECO:0000313|Proteomes:UP000002744};
RX   PubMed=19589076; DOI=10.1094/MPMI-22-8-1011;
RA   Duan Y., Zhou L., Hall D.G., Li W., Doddapaneni H., Lin H., Liu L.,
RA   Vahling C.M., Gabriel D.W., Williams K.P., Dickerman A., Sun Y.,
RA   Gottwald T.;
RT   "Complete genome sequence of citrus huanglongbing bacterium,
RT   'Candidatus Liberibacter asiaticus' obtained through metagenomics.";
RL   Mol. Plant Microbe Interact. 22:1011-1020(2009).
RN   [2] {ECO:0000313|EMBL:ACT56806.1, ECO:0000313|Proteomes:UP000002744}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=psy62 {ECO:0000313|Proteomes:UP000002744};
RX   PubMed=21784907; DOI=10.1128/AEM.05111-11;
RA   Zhou L., Powell C.A., Hoffman M.T., Li W., Fan G., Liu B., Lin H.,
RA   Duan Y.;
RT   "Diversity and plasticity of the intracellular plant pathogen and
RT   insect symbiont, 'Candidatus Liberibacter asiaticus', revealed by
RT   hyper variable prophage genes with intragenic tandem repeats.";
RL   Appl. Environ. Microbiol. 77:6663-6673(2011).
CC   -!- FUNCTION: Catalyzes the interconversion of L-alanine and D-
CC       alanine. May also act on other amino acids. {ECO:0000256|HAMAP-
CC       Rule:MF_01201}.
CC   -!- CATALYTIC ACTIVITY: L-alanine = D-alanine. {ECO:0000256|HAMAP-
CC       Rule:MF_01201, ECO:0000256|SAAS:SAAS00630646}.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01201,
CC         ECO:0000256|PIRSR:PIRSR600821-50,
CC         ECO:0000256|SAAS:SAAS00758845};
CC   -!- PATHWAY: Amino-acid biosynthesis; D-alanine biosynthesis; D-
CC       alanine from L-alanine: step 1/1. {ECO:0000256|HAMAP-
CC       Rule:MF_01201}.
CC   -!- SIMILARITY: Belongs to the alanine racemase family.
CC       {ECO:0000256|HAMAP-Rule:MF_01201, ECO:0000256|SAAS:SAAS00630654}.
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DR   EMBL; CP001677; ACT56806.1; -; Genomic_DNA.
DR   RefSeq; WP_012778552.1; NC_012985.3.
DR   ProteinModelPortal; C6XHR3; -.
DR   STRING; 537021.CLIBASIA_01090; -.
DR   EnsemblBacteria; ACT56806; ACT56806; CLIBASIA_01090.
DR   KEGG; las:CLIBASIA_01090; -.
DR   eggNOG; ENOG4105CJ4; Bacteria.
DR   eggNOG; COG0787; LUCA.
DR   HOGENOM; HOG000031445; -.
DR   KO; K01775; -.
DR   OMA; DTGFNRL; -.
DR   OrthoDB; POG091H022F; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000002744; 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   Gene3D; 2.40.37.10; -; 1.
DR   Gene3D; 3.20.20.10; -; 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   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; SSF50621; 1.
DR   SUPFAM; SSF51419; SSF51419; 1.
DR   TIGRFAMs; TIGR00492; alr; 1.
DR   PROSITE; PS00395; ALANINE_RACEMASE; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000002744};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_01201,
KW   ECO:0000256|SAAS:SAAS00630647};
KW   Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_01201,
KW   ECO:0000256|PIRSR:PIRSR600821-50, ECO:0000256|SAAS:SAAS00722456}.
FT   DOMAIN      235    370       Ala_racemase_C. {ECO:0000259|SMART:
FT                                SM01005}.
FT   ACT_SITE     37     37       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    256    256       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   BINDING     134    134       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01201, ECO:0000256|PIRSR:PIRSR600821-
FT                                52}.
FT   BINDING     315    315       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-52}.
FT   MOD_RES      37     37       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-50}.
SQ   SEQUENCE   370 AA;  40452 MW;  8FB7754FAE0AC312 CRC64;
     MHSNEFLRLK IDLTALKNNW HSMNALSGNA RTAAVVKDNA YGLGCEKIAP ALYNAGVQDF
     FVTSVEEGVK LRLYTPQARI FVLYGIHPGQ EKIIFDTNLI PVISSVPQLT FYSKLMSCGV
     SHPYALQVDT GFNRLGLSLQ EALDFTHNSF NKKLGQLSLI ISHLACADDP SSHVNSVQLE
     RFRTLISHYK GIEASLASSS GILLGPNYHF QLTRPGISLY GGTDKINKSH PMQTVVTAEA
     RIILIRKALA GELVSYGGQK KLTRDSLIAV AAIGYADGYP LTLSGLDSEH SPSVFLGGKG
     FIKGYMVPIL GKITMDMTMF DITDSLSIEV GDYIQIFGPD IKLDDVALAS GTTNYDLLVR
     IGTRYAKFYT
//
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