ID T0GM73_9SPHN Unreviewed; 337 AA.
AC T0GM73;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=alanine racemase {ECO:0000256|ARBA:ARBA00013089};
DE EC=5.1.1.1 {ECO:0000256|ARBA:ARBA00013089};
GN ORFNames=L286_09140 {ECO:0000313|EMBL:EQB04926.1};
OS Sphingobium sp. HDIP04.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=428994 {ECO:0000313|EMBL:EQB04926.1, ECO:0000313|Proteomes:UP000015528};
RN [1] {ECO:0000313|EMBL:EQB04926.1, ECO:0000313|Proteomes:UP000015528}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HDIP04 {ECO:0000313|EMBL:EQB04926.1,
RC ECO:0000313|Proteomes:UP000015528};
RX PubMed=24051321;
RA Mukherjee U., Kumar R., Mahato N.K., Khurana J.P., Lal R.;
RT "Draft Genome Sequence of Sphingobium sp. Strain HDIPO4, an Avid Degrader
RT of Hexachlorocyclohexane.";
RL Genome Announc. 1:e00749-e00713(2013).
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|ARBA:ARBA00000316};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|PIRSR:PIRSR600821-50};
CC -!- SIMILARITY: Belongs to the alanine racemase family.
CC {ECO:0000256|ARBA:ARBA00007880}.
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:EQB04926.1}.
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DR EMBL; ATDO01000078; EQB04926.1; -; Genomic_DNA.
DR AlphaFoldDB; T0GM73; -.
DR PATRIC; fig|428994.3.peg.1746; -.
DR Proteomes; UP000015528; Unassembled WGS sequence.
DR GO; GO:0008784; F:alanine racemase activity; IEA:UniProtKB-EC.
DR GO; GO:0006522; P:alanine metabolic process; IEA:InterPro.
DR CDD; cd00430; PLPDE_III_AR; 1.
DR Gene3D; 3.20.20.10; Alanine 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; IPR020622; Ala_racemase_pyridoxalP-BS.
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 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.
DR PROSITE; PS50007; PIPLC_X_DOMAIN; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR600821-50}.
FT DOMAIN 216..337
FT /note="Alanine racemase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01005"
FT BINDING 121
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR600821-52"
FT BINDING 285
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR600821-52"
FT MOD_RES 27
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR600821-50"
SQ SEQUENCE 337 AA; 36333 MW; CE26FF23909DC37C CRC64;
MDEGALLSNW RWLKRQGGDA ACGAAIKADG YGLGAVEVMR RLLGAGCRDF FVSNWAEAAV
LEPLVTEGVS LSVLHGVREE DLAVALASRA RPVLCTEWQI ARWRHAGGGP CDVMVDTGMN
RLGLDWRGDV PARLAGLEIA NLMSHLACAD EDGPLSPVQL ERFSALRGQV KAARYSLANS
AGICMGADYA FDMTRPGIAL YGGVPRREAA GHIRQVVVPE AQVLQRRRVR AGDTIGYNAT
YRAPKDMQIA VLNLGYADGY LRCFSGRGSM SAGGRHLPVV GRISMDLTAV DVSGLPDISE
EDWLEVDYKL VDAAAASGLS QYELLTGLGA RFDRVWR
//
