ID A0A3R8PFU0_9CORY Unreviewed; 648 AA.
AC A0A3R8PFU0;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
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=CXF42_05180 {ECO:0000313|EMBL:RRQ04108.1};
OS Corynebacterium bovis.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=36808 {ECO:0000313|EMBL:RRQ04108.1, ECO:0000313|Proteomes:UP000278422};
RN [1] {ECO:0000313|EMBL:RRQ04108.1, ECO:0000313|Proteomes:UP000278422}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=16-2004 {ECO:0000313|EMBL:RRQ04108.1,
RC ECO:0000313|Proteomes:UP000278422};
RA Gulvik C.A.;
RT "Twenty Corynebacterium bovis Genomes.";
RL Submitted (JAN-2018) 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 -!- FUNCTION: Required for the formation of a threonylcarbamoyl group on
CC adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning
CC with adenine. Is involved in the transfer of the threonylcarbamoyl
CC moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37,
CC together with TsaD and TsaB. TsaE seems to play an indirect role in the
CC t(6)A biosynthesis pathway, possibly in regulating the core enzymatic
CC function of TsaD. {ECO:0000256|ARBA:ARBA00024908}.
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RRQ04108.1}.
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DR EMBL; PQNQ01000011; RRQ04108.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3R8PFU0; -.
DR UniPathway; UPA00042; UER00497.
DR Proteomes; UP000278422; 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:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0030632; P:D-alanine biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0002949; P:tRNA threonylcarbamoyladenosine modification; IEA:InterPro.
DR CDD; cd00430; PLPDE_III_AR; 1.
DR Gene3D; 3.20.20.10; Alanine racemase; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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; IPR027417; P-loop_NTPase.
DR InterPro; IPR029066; PLP-binding_barrel.
DR InterPro; IPR003442; T6A_TsaE.
DR NCBIfam; TIGR00150; T6A_YjeE; 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 Pfam; PF02367; TsaE; 1.
DR PRINTS; PR00992; ALARACEMASE.
DR SMART; SM01005; Ala_racemase_C; 1.
DR SUPFAM; SSF50621; Alanine racemase C-terminal domain-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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:UP000278422};
KW Transferase {ECO:0000313|EMBL:RRQ04108.1}.
FT DOMAIN 285..414
FT /note="Alanine racemase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01005"
FT REGION 255..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 417..444
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 547..583
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 44
FT /note="Proton acceptor; specific for D-alanine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT ACT_SITE 306
FT /note="Proton acceptor; specific for L-alanine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT BINDING 150
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT ECO:0000256|PIRSR:PIRSR600821-52"
FT BINDING 354
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT ECO:0000256|PIRSR:PIRSR600821-52"
FT MOD_RES 44
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT ECO:0000256|PIRSR:PIRSR600821-50"
SQ SEQUENCE 648 AA; 65889 MW; 29410EF465C3843C CRC64;
MPVSDIQAGP HSLAELVVDL GAVAHNVRRL RALAAPARLM AVVKADGYNM GARAVALTAL
DHGADELGVA TVGEGLETLA VLRDAGRTAP VTAWMWYPGE PLDDAVAAGL TLGIPSLEHA
RALTAVATDR ARPGQSPVRA TLMADTGLSR SGIAPGEWGE VLDLVAAAAR TGSVEVTGVM
SHLSGADDAT SPATDIQATR FRRAIDDCRA RGLDVPVNHI ANTPATLTRP DLRFDMVRPG
VGVYGVDPCA GGGAGEPGAG DGADGAVGAV EPGAAGDGGR GLRPVATLRA RVTTTRLVPR
GESVGYGGLW TADRDTRTAV VAIGYADGIP RALTGAFDVT VRGRRYRQIG RVSMDQIVVD
LGPADGPEPE VRPGDWAVIF GEGGATLSEA ARALGTIDYE VLTLPRTRVR RRYIPAGEGE
GAGAGGVDGR EGDAAGAVGA GDGAGVGVGT ETPVNPGAPD GTVAVPTAEA MRQVGEAVGR
ELRAGDVVVL TGPLGAGKTT LTQGIARGMG VTGRVQSPTF TVVREHRPSG DGPGLLHMDA
YRLLDGLRDD DAHGTGETGS AGQPEGTGSA GQGAGHGESA ARSAAVLDAL ESLDLDGDLT
DHALVAEWGE GVVEPLGTRV LHITLSRDGV DAPGDDEART LAWRWTGR
//
