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Database: UniProt/TrEMBL
Entry: C4LKV7_CORK4
LinkDB: C4LKV7_CORK4
Original site: C4LKV7_CORK4 
ID   C4LKV7_CORK4            Unreviewed;       615 AA.
AC   C4LKV7;
DT   07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   07-JUL-2009, sequence version 1.
DT   27-SEP-2017, entry version 64.
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=ckrop_1741 {ECO:0000313|EMBL:ACR18462.1};
OS   Corynebacterium kroppenstedtii (strain DSM 44385 / JCM 11950 / CIP
OS   105744 / CCUG 35717).
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=645127 {ECO:0000313|EMBL:ACR18462.1, ECO:0000313|Proteomes:UP000001473};
RN   [1] {ECO:0000313|EMBL:ACR18462.1, ECO:0000313|Proteomes:UP000001473}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44385 / JCM 11950 / CIP 105744 / CCUG 35717
RC   {ECO:0000313|Proteomes:UP000001473};
RX   PubMed=18430482; DOI=10.1016/j.jbiotec.2008.03.004;
RA   Tauch A., Schneider J., Szczepanowski R., Tilker A., Viehoever P.,
RA   Gartemann K.-H., Arnold W., Blom J., Brinkrolf K., Brune I.,
RA   Goetker S., Weisshaar B., Goesmann A., Droege M., Puehler A.;
RT   "Ultrafast pyrosequencing of Corynebacterium kroppenstedtii DSM44385
RT   revealed insights into the physiology of a lipophilic corynebacterium
RT   that lacks mycolic acids.";
RL   J. Biotechnol. 136:22-30(2008).
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}.
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}.
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DR   EMBL; CP001620; ACR18462.1; -; Genomic_DNA.
DR   ProteinModelPortal; C4LKV7; -.
DR   STRING; 645127.ckrop_1741; -.
DR   EnsemblBacteria; ACR18462; ACR18462; ckrop_1741.
DR   KEGG; ckp:ckrop_1741; -.
DR   eggNOG; ENOG4105CJ4; Bacteria.
DR   eggNOG; COG0787; LUCA.
DR   eggNOG; COG0802; LUCA.
DR   HOGENOM; HOG000031444; -.
DR   KO; K01775; -.
DR   OMA; MEVAING; -.
DR   OrthoDB; POG091H022F; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000001473; 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   GO; GO:0002949; P:tRNA threonylcarbamoyladenosine modification; IEA:InterPro.
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; IPR027417; P-loop_NTPase.
DR   InterPro; IPR029066; PLP-binding_barrel.
DR   InterPro; IPR003442; T6A_TsaE.
DR   Pfam; PF00842; Ala_racemase_C; 1.
DR   Pfam; PF01168; Ala_racemase_N; 1.
DR   Pfam; PF02367; TsaE; 1.
DR   PRINTS; PR00992; ALARACEMASE.
DR   SMART; SM01005; Ala_racemase_C; 1.
DR   SUPFAM; SSF50621; SSF50621; 1.
DR   SUPFAM; SSF51419; SSF51419; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00492; alr; 1.
DR   TIGRFAMs; TIGR00150; T6A_YjeE; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000001473};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_01201,
KW   ECO:0000256|SAAS:SAAS00630647, ECO:0000313|EMBL:ACR18462.1};
KW   Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_01201,
KW   ECO:0000256|PIRSR:PIRSR600821-50, ECO:0000256|SAAS:SAAS00722456};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001473}.
FT   DOMAIN      295    437       Ala_racemase_C. {ECO:0000259|SMART:
FT                                SM01005}.
FT   ACT_SITE     67     67       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    316    316       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   BINDING     175    175       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01201, ECO:0000256|PIRSR:PIRSR600821-
FT                                52}.
FT   BINDING     364    364       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-52}.
FT   MOD_RES      67     67       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-50}.
SQ   SEQUENCE   615 AA;  64933 MW;  DFB31D002B5F661A CRC64;
     MMSMPIQSSS HAVSSDHLSA GGNDAALPGL LTMTIDRDAL AHNAQAVARN AQLANPDHPA
     ELMAVVKANG YNHGAVEAAR VFLANGATQL GVATITEAVE LRQAGISAPI LAWIWNADDH
     VSVKAALDYG IDLGVPTLAH IRAIVDEATE RKRSQEDWEF VPPRVTVMVD SGLSRSGISP
     DQWDDALKEL SAASSDSIID VTGAFTHLAS ADAADNPSNN RQKAQFDAAI EELQAAGIPV
     RINHMCNSPA SVTRPDMFYQ MVRPGVALYG MDPLEEPADR SASTGSSLVS QLKPAMTLSA
     PIVAKRLVKA GESVSYGGTW TADVDTVTGV VPAGYADGIP RALSGRMEVA INGRRYPQIG
     RVCMDQIVVA LGPAGSKQAS AVHQGDEAVI FGPPGECIGS DGKPASLPTA TELAETLGTI
     HYEILTSPHT RVHRRYVGRG LVDGRVRVRN AEATQTLAES IAHALRPGDV VVLDGPLGAG
     KTTFTQGLAR GLHVSGRVTS PTFTIAREHP GPVPFIHVDA YRLLGDTTTD PIGALDSLDL
     DTRIPDSIVV AEWAADMADA LEQDYLLIRL ERATGGSERP AGNDASAGGD TSAPADPVDF
     DEDEPRVISW TWVRR
//
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