GenomeNet

Database: UniProt/TrEMBL
Entry: A0A097IE10_9CORY
LinkDB: A0A097IE10_9CORY
Original site: A0A097IE10_9CORY 
ID   A0A097IE10_9CORY        Unreviewed;       363 AA.
AC   A0A097IE10;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   RecName: Full=Alanine racemase {ECO:0000256|HAMAP-Rule:MF_01201};
DE            EC=5.1.1.1 {ECO:0000256|HAMAP-Rule:MF_01201};
GN   ORFNames=CDOO_03150 {ECO:0000313|EMBL:AIT60350.1};
OS   Corynebacterium doosanense CAU 212 = DSM 45436.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=558173 {ECO:0000313|EMBL:AIT60350.1, ECO:0000313|Proteomes:UP000029914};
RN   [1] {ECO:0000313|EMBL:AIT60350.1, ECO:0000313|Proteomes:UP000029914}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CAU 212 {ECO:0000313|EMBL:AIT60350.1,
RC   ECO:0000313|Proteomes:UP000029914};
RA   Schaffert L., Albersmeier A., Kalinowski J., Ruckert C.;
RT   "Complete genome sequence of Corynebacterium doosanense CAU 212(T) (=DSM
RT   45436(T)), isolated from activated sludge.";
RL   Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP006764; AIT60350.1; -; Genomic_DNA.
DR   RefSeq; WP_018021228.1; NZ_CP006764.1.
DR   AlphaFoldDB; A0A097IE10; -.
DR   STRING; 558173.CDOO_03150; -.
DR   KEGG; cdo:CDOO_03150; -.
DR   eggNOG; COG0787; Bacteria.
DR   HOGENOM; CLU_028393_0_0_11; -.
DR   OrthoDB; 9813814at2; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000029914; 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}; Reference proteome {ECO:0000313|Proteomes:UP000029914}.
FT   DOMAIN          237..363
FT                   /note="Alanine racemase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01005"
FT   ACT_SITE        35
FT                   /note="Proton acceptor; specific for D-alanine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT   ACT_SITE        258
FT                   /note="Proton acceptor; specific for L-alanine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT   BINDING         132
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT                   ECO:0000256|PIRSR:PIRSR600821-52"
FT   BINDING         306
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT                   ECO:0000256|PIRSR:PIRSR600821-52"
FT   MOD_RES         35
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT                   ECO:0000256|PIRSR:PIRSR600821-50"
SQ   SEQUENCE   363 AA;  38928 MW;  E1BA1547AB6D6173 CRC64;
     MSQLRARIDL DAIAHNTRAV KARLSEGTRL MAVVKADGYN HGAAEVAAVM AENGADAFGV
     ATAAEGSRLR ESGVDKPILA WLWSPDDPGD EVTEALASGV ELGVPSLVHL RALVAMEIPA
     RICLKLETGM HRSGIDEAAW YEAFSLARDT PFLTVTGIFS HLARADEPDD PANDLQAANF
     ARAIEIGRSL GLELPVNHLC NSPATLSRPD LHHDQVRVGL ALYGMNPLPG EYDLRPAMTW
     AADVVSVKPL APGDGVSYGH TFTADRQGYT AVLPVGYADG LPRAMQDKLQ VTIAGRRYQQ
     IGRVCMDQIV VDLGDNPHAV MPGAEAVLFG PGAMSVDEFA DALGTINYEV ACLPKGRTRR
     QYR
//
DBGET integrated database retrieval system