ID A0A1F1ZMI8_9CORY Unreviewed; 599 AA.
AC A0A1F1ZMI8;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 35.
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=HMPREF3098_07785 {ECO:0000313|EMBL:OFT88713.1};
OS Corynebacterium sp. HMSC28B08.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1581066 {ECO:0000313|EMBL:OFT88713.1, ECO:0000313|Proteomes:UP000177449};
RN [1] {ECO:0000313|EMBL:OFT88713.1, ECO:0000313|Proteomes:UP000177449}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HMSC28B08 {ECO:0000313|EMBL:OFT88713.1,
RC ECO:0000313|Proteomes:UP000177449};
RA Evans L.H., Alamgir A., Owens N., Weber N.D., Virtaneva K., Barbian K.,
RA Babar A., Rosenke K.;
RL Submitted (APR-2016) 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:OFT88713.1}.
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DR EMBL; LWOT01000055; OFT88713.1; -; Genomic_DNA.
DR RefSeq; WP_070434679.1; NZ_KV786170.1.
DR AlphaFoldDB; A0A1F1ZMI8; -.
DR STRING; 1581066.HMPREF3098_07785; -.
DR UniPathway; UPA00042; UER00497.
DR Proteomes; UP000177449; 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 GO; GO:0002949; P:tRNA threonylcarbamoyladenosine modification; IEA:InterPro.
DR CDD; cd00267; ABC_ATPase; 1.
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; TIGR00492; alr; 1.
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; 2.
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; 2.
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}.
FT DOMAIN 300..429
FT /note="Alanine racemase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01005"
FT REGION 133..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 155..170
FT /note="Polar residues"
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 321
FT /note="Proton acceptor; specific for L-alanine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT BINDING 188
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT ECO:0000256|PIRSR:PIRSR600821-52"
FT BINDING 369
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 599 AA; 62857 MW; DA8F1D1BFFA3DACC CRC64;
MYQPLSVPDE HALAEVVVDL SAIRANVSLF VDAASSAEVM TVVKADAYNH GAVSVARACL
EGGATQLGTA TVGEALCLRE AGVTAPITAW MWIPGEDLSA AVRAGITIGV PSLAHAESLV
ALAQRMAAEQ SSGVTAGVEQ PANPAAGAEQ AGSAAGAEQT GSAAGSNRVV SPNQPIPITL
MADTGLSRSG ITPDQWTAVV ELIAQHRDLL DVKGVMSHLA SADDSARAAF TDVQNRRFHQ
AIEVCREHGI HPETNHIANT PAALTRPDLH HQMVRPGVGI YGIDPVVGGS GGNAAQLRPA
ITFRAKVITT KVIRTGESVS YGGTWTATRD TRTAVVAAGY ADGVPRSASG NFQVGIGGKL
YPQIGRVCMD QIVVNLGDAH EPTEVEPGQW ATIFGEGGIS ASELAAAAGT IDYEILTMPR
GARVRRRWVG EEREQLSLAY NNGHATVPTP DDMREVGRRI GGQLDAGTVV VLTGPLGAGK
TTLTQGIAGG LGVKGRVQSP TFTIVRTHKP GAEDRPGMLH MDAYRLLGAD VSDGVEPGRH
ANREDVLDAL EALDIDADLD RAVIVAEWGR GVVEELSNKV LDIEIDRAGD ERIVRWEWR
//
