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Database: UniProt/TrEMBL
Entry: A0A0B6F0U8_9CORY
LinkDB: A0A0B6F0U8_9CORY
Original site: A0A0B6F0U8_9CORY 
ID   A0A0B6F0U8_9CORY        Unreviewed;       364 AA.
AC   A0A0B6F0U8;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 40.
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:AJI78075.1};
GN   ORFNames=CSING_02625 {ECO:0000313|EMBL:AJI78075.1};
OS   Corynebacterium singulare.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=161899 {ECO:0000313|EMBL:AJI78075.1, ECO:0000313|Proteomes:UP000031890};
RN   [1] {ECO:0000313|EMBL:AJI78075.1, ECO:0000313|Proteomes:UP000031890}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBS B52218 {ECO:0000313|EMBL:AJI78075.1};
RX   PubMed=25814602;
RA   Merten M., Brinkrolf K., Albersmeier A., Kutter Y., Ruckert C., Tauch A.;
RT   "Complete Genome Sequence and Annotation of Corynebacterium singulare DSM
RT   44357, Isolated from a Human Semen Specimen.";
RL   Genome Announc. 3:0-0(2015).
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}.
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DR   EMBL; CP010827; AJI78075.1; -; Genomic_DNA.
DR   RefSeq; WP_042529413.1; NZ_CP010827.1.
DR   AlphaFoldDB; A0A0B6F0U8; -.
DR   STRING; 161899.CSING_02625; -.
DR   KEGG; csx:CSING_02625; -.
DR   HOGENOM; CLU_028393_0_0_11; -.
DR   OrthoDB; 9813814at2; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000031890; 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          232..358
FT                   /note="Alanine racemase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01005"
FT   ACT_SITE        32
FT                   /note="Proton acceptor; specific for D-alanine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT   ACT_SITE        253
FT                   /note="Proton acceptor; specific for L-alanine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT   BINDING         126
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT                   ECO:0000256|PIRSR:PIRSR600821-52"
FT   BINDING         301
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT                   ECO:0000256|PIRSR:PIRSR600821-52"
FT   MOD_RES         32
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT                   ECO:0000256|PIRSR:PIRSR600821-50"
SQ   SEQUENCE   364 AA;  38485 MW;  0050CEAE86D7C2A0 CRC64;
     MLRTTVDLAA IAHNVAVVKE AVAPARLMCV VKADAYGHGI ERVAPVMEEA GADAFGVATL
     SEAVALRQVI PTAPIAGWLW DPHEDLTPAL DAGIQIGIPS LEHARALIAT GRHAEAFVMV
     ETGMHRSGVD KHEWSETFAV LRDAPTITVL GLMSHFACAD DPTHPHNDHQ EAEFREALSC
     AREVGLECPI NHLANSPAAL TRPSARFDQV RVGVALYGLE PVAGREHGLI PAMSWESSVV
     AVKPISAGES TSYGLTWTAE SDRYLATVAV GYADGLPRDV QGALQVGLGG ELYPQVGRVC
     MDQIIVDLGS NPHGVEAGDT AVLFGRGGMS ATELADAAGT INYEIVCRPT GRTTRIYCEG
     TSNA
//
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