ID A0A267THW1_9BACT Unreviewed; 839 AA.
AC A0A267THW1;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
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=BWI92_03940 {ECO:0000313|EMBL:PAC32375.1};
OS Flectobacillus sp. BAB-3569.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC Flectobacillus.
OX NCBI_TaxID=1509483 {ECO:0000313|EMBL:PAC32375.1, ECO:0000313|Proteomes:UP000215844};
RN [1] {ECO:0000313|EMBL:PAC32375.1, ECO:0000313|Proteomes:UP000215844}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BAB-3569 {ECO:0000313|EMBL:PAC32375.1,
RC ECO:0000313|Proteomes:UP000215844};
RA Dhebar S., Dhebar S., Bhargava P., Bagatharia S.B., Soni S., Joshi M.N.;
RT "Flectobacillus sp. BAB-3569 genome sequencing.";
RL Submitted (JUN-2017) 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 -!- 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:PAC32375.1}.
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DR EMBL; NJFZ01000005; PAC32375.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A267THW1; -.
DR OrthoDB; 9801978at2; -.
DR UniPathway; UPA00042; UER00497.
DR Proteomes; UP000215844; Unassembled WGS sequence.
DR GO; GO:0016881; F:acid-amino acid ligase activity; IEA:InterPro.
DR GO; GO:0008784; F:alanine racemase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR GO; GO:0030632; P:D-alanine biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd00430; PLPDE_III_AR; 1.
DR Gene3D; 3.20.20.10; Alanine racemase; 1.
DR Gene3D; 3.90.190.20; Mur ligase, C-terminal domain; 1.
DR Gene3D; 3.40.1190.10; Mur-like, catalytic domain; 1.
DR Gene3D; 3.40.1390.10; MurE/MurF, N-terminal domain; 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; IPR036565; Mur-like_cat_sf.
DR InterPro; IPR036615; Mur_ligase_C_dom_sf.
DR InterPro; IPR013221; Mur_ligase_cen.
DR InterPro; IPR035911; MurE/MurF_N.
DR InterPro; IPR029066; PLP-binding_barrel.
DR NCBIfam; TIGR00492; alr; 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; PF08245; Mur_ligase_M; 1.
DR PRINTS; PR00992; ALARACEMASE.
DR SMART; SM01005; Ala_racemase_C; 1.
DR SUPFAM; SSF50621; Alanine racemase C-terminal domain-like; 1.
DR SUPFAM; SSF53623; MurD-like peptide ligases, catalytic domain; 1.
DR SUPFAM; SSF53244; MurD-like peptide ligases, peptide-binding domain; 1.
DR SUPFAM; SSF63418; MurE/MurF N-terminal domain; 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 Ligase {ECO:0000313|EMBL:PAC32375.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, ECO:0000256|HAMAP-
KW Rule:MF_01201}; Reference proteome {ECO:0000313|Proteomes:UP000215844}.
FT DOMAIN 712..837
FT /note="Alanine racemase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01005"
FT ACT_SITE 508
FT /note="Proton acceptor; specific for D-alanine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT ACT_SITE 733
FT /note="Proton acceptor; specific for L-alanine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT BINDING 605
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT ECO:0000256|PIRSR:PIRSR600821-52"
FT BINDING 782
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT ECO:0000256|PIRSR:PIRSR600821-52"
FT MOD_RES 508
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT ECO:0000256|PIRSR:PIRSR600821-50"
SQ SEQUENCE 839 AA; 94425 MW; 214D4412BFC4219A CRC64;
MKFQTAPIST HAQYLLNDSR QLSSPSSSIF FAIKGLHHDG HQYLDDLYRK GVREFVVEKS
ACNIGVMREL SQMPEAKVWQ VEDSILSMQE VAAQHRAQFT IPVIGVTGSN GKTVVKEWLS
QLLANRFQIV KSPKSYNSQI GVPLSVWQMN KAHTLAIFEA GISRPEEMEA LQKVIQPTIG
IFTNIGTAHN EFFAETSQKI REKMKLFQQS KTLIYCSDYV EIDEIVKKEF IFENPSCKIL
SWSRVLPFGI RVDWEVGLQN TLVTLQLDDP DTEKEDLPFQ GGHAMKLDVP FTDEASIENA
IHCIVSMIHL GYNELEIQAR LQILRPISMR LEMKQGVRGN YLIDDTYNND LAGLTIALNF
LNQQKQRETK VLILSDLLET GVVESELYKH IAHLVKAKHL DMVIGIGEII TRNCGLFSIP
AKNGVHEGAL HFFRTTQDFL ESRLIKEIKD SVILVKGARK FGFEQVVSKL VKKTHGTILE
INLDAITHNL NYYRDKIGQQ TKIMVMVKAF AYGAGSTEVA NLLQFHGVDY LTVAYADEGV
ALRQNGVYLP IMVMNPSPND FEQIIQYNLE PEIYSKRILR EFSEYIDEHH LTAKIHIKLD
TGMHRLGFEK HELPALLEVL TCNPNLWVST IFSHLVGADG AEHDDFTRNQ AALYTEMANE
ISEAIGYFPS RHLANSAGIA RFPEARLDMV RLGIGLYGVA ATPEDQAQLQ TVGTLKTVIS
QIKTVDANET VGYSRKGILN RKTKTATIAI GYADGFDRGF SRGNGEVLVH GVRCKVIGNI
CMDMCMIDVT DVPNVQEGDE VIIFGKDLSI IELAQKIDTI PYEILTNVSE RVKRVFFQV
//
