ID A0A1L7AKZ2_9PROT Unreviewed; 396 AA.
AC A0A1L7AKZ2;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-SEP-2017, entry version 5.
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=RGI145_17215 {ECO:0000313|EMBL:APT59445.1};
OS Roseomonas gilardii.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Roseomonas.
OX NCBI_TaxID=257708 {ECO:0000313|EMBL:APT59445.1, ECO:0000313|Proteomes:UP000185494};
RN [1] {ECO:0000313|EMBL:APT59445.1, ECO:0000313|Proteomes:UP000185494}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=U14-5 {ECO:0000313|EMBL:APT59445.1,
RC ECO:0000313|Proteomes:UP000185494};
RA Fomenkov A., Akimov V.N., Vasilyeva L.V., Andersen D., Vincze T.,
RA Roberts R.J.;
RT "Complete Genome and Methylome Analysis of Psychrotrophic Bacterial
RT Isolates from Antarctic Lake Untersee.";
RL Submitted (MAY-2016) 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}.
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DR EMBL; CP015583; APT59445.1; -; Genomic_DNA.
DR RefSeq; WP_075800162.1; NZ_CP015583.1.
DR KEGG; rgi:RGI145_17215; -.
DR KO; K01775; -.
DR UniPathway; UPA00042; UER00497.
DR Proteomes; UP000185494; Chromosome 1.
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:UP000185494};
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 250 376 Ala_racemase_C. {ECO:0000259|SMART:
FT SM01005}.
FT ACT_SITE 45 45 Proton acceptor; specific for D-alanine.
FT {ECO:0000256|HAMAP-Rule:MF_01201}.
FT ACT_SITE 271 271 Proton acceptor; specific for L-alanine.
FT {ECO:0000256|HAMAP-Rule:MF_01201}.
FT BINDING 149 149 Substrate. {ECO:0000256|HAMAP-Rule:
FT MF_01201, ECO:0000256|PIRSR:PIRSR600821-
FT 52}.
FT BINDING 319 319 Substrate; via amide nitrogen.
FT {ECO:0000256|HAMAP-Rule:MF_01201,
FT ECO:0000256|PIRSR:PIRSR600821-52}.
FT MOD_RES 45 45 N6-(pyridoxal phosphate)lysine.
FT {ECO:0000256|HAMAP-Rule:MF_01201,
FT ECO:0000256|PIRSR:PIRSR600821-50}.
SQ SEQUENCE 396 AA; 42188 MW; 90E6A3FCA8FB159F CRC64;
MHSPARERLW PAAGAILTID LGAIRANWRW LRDRVAPAAC GAVLKADAYG LGAALVGPAL
LAEGCRDFFV AHLEEGIALR QDLRGQPGAE EARIHVMHGL FDGTEREALA HGLIPVLNSL
EQVAGWAGLS RAEGRRLPAW LQLDTGMARF GFSVGELDRL LEDGRDLAAV EPIRVMSHLA
CADEPGHPAN AAQLGAFNAM RRRLPHLPTS LAASSGIFLD RAWHGDLVRP GVALHGVAPL
PRGENPLRPV LRLDARVVQT RSVPAGTAVG YGHSFTTRTP SRLATIAVGY ADGFLRSASN
RGRAMWKGMP MPILGRVSMD SIVLDASALP ENALRPGDTV ELIGPDHDLE AVAEAAGTIP
YEILTSLGQR YHRRYETGAP GSSGEVLQPT GPAVTA
//
