ID A0A1H6VGB8_9BACT Unreviewed; 823 AA.
AC A0A1H6VGB8;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
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=SAMN05192553_10218 {ECO:0000313|EMBL:SEJ02776.1};
OS Cyclobacterium xiamenense.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC Cyclobacterium.
OX NCBI_TaxID=1297121 {ECO:0000313|EMBL:SEJ02776.1, ECO:0000313|Proteomes:UP000199403};
RN [1] {ECO:0000313|Proteomes:UP000199403}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBRC-M 10761 {ECO:0000313|Proteomes:UP000199403};
RA Varghese N., Submissions S.;
RL Submitted (OCT-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 -!- 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; FNZH01000002; SEJ02776.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H6VGB8; -.
DR STRING; 1416801.SAMN05192553_10218; -.
DR UniPathway; UPA00042; UER00497.
DR Proteomes; UP000199403; 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 Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, ECO:0000256|HAMAP-
KW Rule:MF_01201}.
FT DOMAIN 697..821
FT /note="Alanine racemase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01005"
FT ACT_SITE 496
FT /note="Proton acceptor; specific for D-alanine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT ACT_SITE 718
FT /note="Proton acceptor; specific for L-alanine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT BINDING 590
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT ECO:0000256|PIRSR:PIRSR600821-52"
FT BINDING 767
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT ECO:0000256|PIRSR:PIRSR600821-52"
FT MOD_RES 496
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT ECO:0000256|PIRSR:PIRSR600821-50"
SQ SEQUENCE 823 AA; 92077 MW; 6C5727AD36898F98 CRC64;
MIDPIDFNAF SVNHSGDYLP GSAPAQIQRV SIDSRNLQNG TSTLFVALEG TRRSGWHFAA
DAYRQQVRNF ILPAAAHSPE LQTSLSGSNL LFCQDPLHAL QDLAQMNRHA FKGTVVGITG
SNGKTIVKEW LAQVLSENYR VWKSPKSYNS QLGVPLSVLG MESSHQVALL EAGISQPGEM
KRLEAIIQPR LGIFTTIGTA HDENFENLEQ KIAEKCVLFA DCRFVIYRKD VEKISGYLEQ
HFPPEVRISW SEKPGADYML TVKPDGKKGS RLLLLGNDLS TYTFTTTFRD PASLENIRHV
IVSGLVLGMS AQSVQRGLDL LHAVDMRLTA KQGINRCRIL DDSYNNDLAG LEIALEFMNQ
QGKPAGKKVL ILSEMLQEGK QSVVHERIAR MITHYGIDRF VGVGKNFDSH KGIFPEQRAF
YPDTDTLLER LSELNLQEDL ILVKGARAFH FERVVRALEA QVHDTVLEIN LNCLRHNFDH
YRAQLKPGTK VMVMVKAFAY GSGSAEIAHH LQQIGADYLS VAYPDEGVYL RERGVELPIM
VMNSAARHLD LLLRYRLEPV VYDLQTLREL ADTATENLSI HLELDTGMRR LGMEEMDLEA
TVTLLQQHPH IQMAGLFSHL AAADEAAHEA FSRQQLALFD RWSRFLMQRL GCRPLRHVLN
SAGIIRFPEY ALDMVRLGIG LFGVEINGME QEKLQPAVSL KTVVSQVRKL KKGETIGYGR
RGRMHADGEI ATLAIGYADG YDRRFGNGQA YVLIKGNKAR TIGTICMDMC MVDVTGMDVR
EGDAVMLFGE DPSLQQLAEC IGTIPYELLT GIGRRVKRLY VLD
//
