ID A0A163CRB2_9MICO Unreviewed; 459 AA.
AC A0A163CRB2;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE SubName: Full=Adenylosuccinate lyase {ECO:0000313|EMBL:KZE33006.1};
GN ORFNames=AVW09_06360 {ECO:0000313|EMBL:KZE33006.1};
OS Microbacterium sp. T32.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=1776083 {ECO:0000313|EMBL:KZE33006.1, ECO:0000313|Proteomes:UP000076494};
RN [1] {ECO:0000313|Proteomes:UP000076494}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T32 {ECO:0000313|Proteomes:UP000076494};
RA Hong K.W.;
RT "Whole genome sequencing of Bhargavaea cecembensis T14.";
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes two reactions in de novo purine nucleotide
CC biosynthesis. Catalyzes the breakdown of 5-aminoimidazole- (N-
CC succinylocarboxamide) ribotide (SAICAR or 2-[5-amino-1-(5-phospho-beta-
CC D-ribosyl)imidazole-4-carboxamido]succinate) to 5-aminoimidazole-4-
CC carboxamide ribotide (AICAR or 5-amino-1-(5-phospho-beta-D-
CC ribosyl)imidazole-4-carboxamide) and fumarate, and of adenylosuccinate
CC (ADS or N(6)-(1,2-dicarboxyethyl)-AMP) to adenosine monophosphate (AMP)
CC and fumarate. {ECO:0000256|ARBA:ARBA00025012}.
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:KZE33006.1}.
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DR EMBL; LQQP01000077; KZE33006.1; -; Genomic_DNA.
DR RefSeq; WP_063259018.1; NZ_LQQP01000077.1.
DR AlphaFoldDB; A0A163CRB2; -.
DR STRING; 1776083.AVW09_06360; -.
DR OrthoDB; 9768878at2; -.
DR Proteomes; UP000076494; Unassembled WGS sequence.
DR GO; GO:0004018; F:N6-(1,2-dicarboxyethyl)AMP AMP-lyase (fumarate-forming) activity; IEA:InterPro.
DR GO; GO:0006188; P:IMP biosynthetic process; IEA:InterPro.
DR Gene3D; 1.10.40.30; Fumarase/aspartase (C-terminal domain); 1.
DR Gene3D; 1.20.200.10; Fumarase/aspartase (Central domain); 1.
DR Gene3D; 1.10.275.10; Fumarase/aspartase (N-terminal domain); 1.
DR InterPro; IPR024083; Fumarase/histidase_N.
DR InterPro; IPR020557; Fumarate_lyase_CS.
DR InterPro; IPR000362; Fumarate_lyase_fam.
DR InterPro; IPR022761; Fumarate_lyase_N.
DR InterPro; IPR008948; L-Aspartase-like.
DR InterPro; IPR047136; PurB_bact.
DR InterPro; IPR013539; PurB_C.
DR PANTHER; PTHR43411; ADENYLOSUCCINATE LYASE; 1.
DR PANTHER; PTHR43411:SF1; ADENYLOSUCCINATE LYASE; 1.
DR Pfam; PF08328; ASL_C; 1.
DR Pfam; PF00206; Lyase_1; 1.
DR PRINTS; PR00149; FUMRATELYASE.
DR SUPFAM; SSF48557; L-aspartase-like; 1.
DR PROSITE; PS00163; FUMARATE_LYASES; 1.
PE 4: Predicted;
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:KZE33006.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000076494}.
FT DOMAIN 55..308
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT DOMAIN 329..448
FT /note="Adenylosuccinate lyase PurB C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08328"
SQ SEQUENCE 459 AA; 50113 MW; 71C9B74115B682EC CRC64;
MSALPPQPLS PLDGRYFATV SEIGDYLSEA GLNRARVEVE VEWLLALTDR SLFGTSPVSD
ADRARLRALY EEFGADEIAW LKEKEAVTRH DVKAVEYLVR DRLDSLGLTA LAELTHFACT
SEDINSTAYA LTVQRAVQRV WLPKLRAVTA ALAELAVEHR DAAMLSRTHG QPATPTTMGK
EIGVFAWRLE RVIRQLDAGE YLAKFSGATG TWSAHVAAEP DVDWPALTRE FIESLGLGFN
PVTTQIESHD WQVELYDRAR HAGGILHNLA TDIWTYISLG YFTQIPVAGA TGSSTMPHKI
NPIRFENAEA NLEIAGGLFA TLASTLVTSR LQRDLTDSTT QRNIGVAFGH SLLALDNLQR
GLTEISLAED VLLADLDANW EVLAEAIQTV VRAEIAAGRS QITDPYALLK DLTRGRRVGA
AELAEFVRGL DIGDAAKERL LALTPATYAG LASRVVDAL
//
