ID B6CBM0_ENTCA Unreviewed; 700 AA.
AC B6CBM0;
DT 25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT 25-NOV-2008, sequence version 1.
DT 24-JAN-2024, entry version 71.
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=vanTc4 {ECO:0000313|EMBL:ABX79415.1};
OS Enterococcus casseliflavus (Enterococcus flavescens).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=37734 {ECO:0000313|EMBL:ABX79415.1};
RN [1] {ECO:0000313|EMBL:ABX79415.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ES852 {ECO:0000313|EMBL:ABX79415.1};
RX PubMed=19216682; DOI=10.1089/mdr.2009.0856;
RA Watanabe S., Kobayashi N., Quinones D., Hayakawa S., Nagashima S.,
RA Uehara N., Watanabe N.;
RT "Genetic diversity of the low-level vancomycin resistance gene vanC-2/vanC-
RT 3 and identification of a novel vanC subtype (vanC-4) in Enterococcus
RT casseliflavus.";
RL Microb. Drug Resist. 15:1-9(2009).
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; EU151753; ABX79415.1; -; Genomic_DNA.
DR RefSeq; WP_063856756.1; NG_048460.1.
DR AlphaFoldDB; B6CBM0; -.
DR UniPathway; UPA00042; UER00497.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
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:0046677; P:response to antibiotic; IEA:InterPro.
DR Gene3D; 3.20.20.10; Alanine racemase; 1.
DR HAMAP; MF_01201; Ala_racemase; 1.
DR InterPro; IPR002656; Acyl_transf_3_dom.
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 InterPro; IPR011248; Serine/alanine_racemase.
DR NCBIfam; TIGR00492; alr; 1.
DR PANTHER; PTHR30511; ALANINE RACEMASE; 1.
DR PANTHER; PTHR30511:SF0; ALANINE RACEMASE, CATABOLIC-RELATED; 1.
DR Pfam; PF01757; Acyl_transf_3; 1.
DR Pfam; PF00842; Ala_racemase_C; 1.
DR Pfam; PF01168; Ala_racemase_N; 1.
DR PIRSF; PIRSF036464; Ser_ala_racem; 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 Membrane {ECO:0000256|SAM:Phobius};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, ECO:0000256|HAMAP-
KW Rule:MF_01201}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..30
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 36..62
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 83..103
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 123..141
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 148..170
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 190..208
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 220..239
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 245..264
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 306..325
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 578..700
FT /note="Alanine racemase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01005"
FT ACT_SITE 373
FT /note="Proton acceptor; specific for D-alanine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT ACT_SITE 599
FT /note="Proton acceptor; specific for L-alanine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT BINDING 467
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT ECO:0000256|PIRSR:PIRSR600821-52"
FT BINDING 648
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT ECO:0000256|PIRSR:PIRSR600821-52"
FT MOD_RES 373
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT ECO:0000256|PIRSR:PIRSR600821-50"
SQ SEQUENCE 700 AA; 78145 MW; F403ADDFE9F12EA3 CRC64;
MKKNQGIEQF RVILAMMVVA IHCLPLHRLW PNGDILITLT LFRIAVPFFF MISGYYVFSD
LATQNSYPAR QRIWLFIKKQ LQVYLIATLL FLPLAWYSGI LGLNMPLDTF IQTLLVNGIL
YHLWYFPAII TGGLLVMGLL TRLSFKQVFF IAVGLYVVGL GGDSWSGLAA QTPITPLYSL
IFQLLDGTRN GIFFAPLFLI LGVLARRFAK KPASPHRYSY LMISLICLLL ESYLLHHFTT
PKHDSMYVFL PFVLLFLFPI IQQWQAPMIW KQAGRLSLWL YLLHPYTIAV THFLSQKLPL
LQNNLINFLV VLGLTIGVVH GLFALQKLLP FPKKTPLHLQ RAAKEFSAPA LLHNLQEIKR
VIPSTTKVMA VVKADAYGCD AQLVARTLER VGVDFFAVAT IEEAIELRRA GIKSRLLILG
YTSAQRAKEL NRYSLIQTIV SEAHGQALAR TGLPIECHLA VDTGMHRLGV APDLETVRRL
YALPSLKITG IFSHLGSSDQ LDTASILRTQ AQIICFDDLL AGLSARNIAY GLTHLQSSYG
ILNYPEKHYD YVRPGILLTG SLSVPNEPTK QKINVQPILT LKALLVDKKT VAAGEAIGYG
LATVFDRPTT IGIVSIGYCD GVPRALSNQG FQLSYQGVLL PQVGLICMDM LLIDLTDYPE
LAVESWLEVI SDWTNTADQA QTIPNELISR LGSRVPSMSK
//
