GenomeNet

Database: UniProt/TrEMBL
Entry: A0A0D8ERC2_ACIBA
LinkDB: A0A0D8ERC2_ACIBA
Original site: A0A0D8ERC2_ACIBA 
ID   A0A0D8ERC2_ACIBA        Unreviewed;       367 AA.
AC   A0A0D8ERC2;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   20-DEC-2017, entry version 30.
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:PAM73359.1};
GN   ORFNames=CAT78_04700 {ECO:0000313|EMBL:OTT64502.1}, CEJ63_08840
GN   {ECO:0000313|EMBL:PAM73359.1};
OS   Acinetobacter baumannii.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Moraxellaceae; Acinetobacter;
OC   Acinetobacter calcoaceticus/baumannii complex.
OX   NCBI_TaxID=470 {ECO:0000313|EMBL:OTT64502.1, ECO:0000313|Proteomes:UP000195094};
RN   [1] {ECO:0000313|EMBL:OTT64502.1, ECO:0000313|Proteomes:UP000195094}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ARLG1899 {ECO:0000313|EMBL:OTT64502.1};
RA   Song R., Chenine A.L., Ruprecht R.M.;
RL   Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:PAM73359.1, ECO:0000313|Proteomes:UP000216072}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AB75 {ECO:0000313|EMBL:PAM73359.1,
RC   ECO:0000313|Proteomes:UP000216072};
RA   Chen Q.;
RT   "Carbapenem-resistant Acinetobacter baumannii strains.";
RL   Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:OTT64502.1}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; NGHY01000027; OTT64502.1; -; Genomic_DNA.
DR   EMBL; NKKG01000025; PAM73359.1; -; Genomic_DNA.
DR   RefSeq; WP_001137862.1; NZ_NQFK01000006.1.
DR   EnsemblBacteria; KMV12025; KMV12025; AB988_1398.
DR   EnsemblBacteria; OBE56926; OBE56926; A7934_15625.
DR   KEGG; abw:BL01_01230; -.
DR   KO; K01775; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000195094; Unassembled WGS sequence.
DR   Proteomes; UP000216072; Unassembled WGS sequence.
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:UP000195094,
KW   ECO:0000313|Proteomes:UP000216072};
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      237    366       Ala_racemase_C. {ECO:0000259|SMART:
FT                                SM01005}.
FT   ACT_SITE     35     35       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    258    258       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   BINDING     130    130       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01201, ECO:0000256|PIRSR:PIRSR600821-
FT                                52}.
FT   BINDING     306    306       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-52}.
FT   MOD_RES      35     35       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-50}.
SQ   SEQUENCE   367 AA;  40538 MW;  FFD9677ED88935CF CRC64;
     MPRPITAVIH RQALQNNLAV VRKAMPNSKV FAVVKANAYG HGIERVYEAF KAADGFALLD
     IEEAKRIRAL GWTGPILLLE GVFSPQDLFD CVQYQLSFTI HSEAQIEWVE QHPYPAQFDV
     FLKMNSGMNR LGFKPQHYVQ AWERLNNLAN VAKITHMMHF SDADGDRFGQ QGIDYQITAF
     EEIVKDLPGE RSVSNSAAIL RYQDQLKSDY VRSGIMLYGS SPDYPTHSIA DWGLQPTMSL
     RSEIISVQHL EPNESVGYGS NFVAEQPMTI GIVACGYADG YQRISPTGTP VLVDSVRTRT
     VGRVSMDMLA VDLTGIESAK VGSEVVLWGQ SSTGVILPID DVAVSSGTVG YELMCAVTAR
     VQFINQV
//
DBGET integrated database retrieval system