UniProt: D4DTZ4

Database: UniProt
Entry: D4DTZ4_NEIEG

LinkDB:  D4DTZ4_NEIEG 
Original site:  D4DTZ4_NEIEG

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Ontology (3)   
   GO (3)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (1)   
   KEGG GENES (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (2)   
   EMBL (2)   
Protein domain (7)   
   InterPro (6)   
   Pfam (1)   
Literature (1)   
   PubMed (1)   
All databases (16)   

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ID   D4DTZ4_NEIEG            Unreviewed;       246 AA.
AC   D4DTZ4;
DT   18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT   18-MAY-2010, sequence version 1.
DT   27-MAR-2024, entry version 74.
DE   RecName: Full=1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase {ECO:0000256|HAMAP-Rule:MF_01014, ECO:0000256|RuleBase:RU003658};
DE            EC=5.3.1.16 {ECO:0000256|HAMAP-Rule:MF_01014, ECO:0000256|RuleBase:RU003658};
DE   AltName: Full=Phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase {ECO:0000256|HAMAP-Rule:MF_01014};
GN   Name=hisA {ECO:0000256|HAMAP-Rule:MF_01014,
GN   ECO:0000313|EMBL:EFE48577.1};
GN   ORFNames=NEIELOOT_02551 {ECO:0000313|EMBL:EFE48577.1}, NELON_04660
GN   {ECO:0000313|EMBL:AJE18252.1};
OS   Neisseria elongata subsp. glycolytica ATCC 29315.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=546263 {ECO:0000313|EMBL:EFE48577.1, ECO:0000313|Proteomes:UP000005536};
RN   [1] {ECO:0000313|EMBL:EFE48577.1, ECO:0000313|Proteomes:UP000005536}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29315 {ECO:0000313|EMBL:EFE48577.1,
RC   ECO:0000313|Proteomes:UP000005536};
RA   Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA   Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA   Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA   Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA   Chinwalla A., Mardis E.R., Wilson R.K.;
RL   Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000031392}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29315 {ECO:0000313|Proteomes:UP000031392};
RA   Veyrier F.J., Taha M.-K.;
RT   "Complete Genome sequence of Neisseria elongata subsp. glycolytica.";
RL   Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:AJE18252.1, ECO:0000313|Proteomes:UP000031392}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29315 {ECO:0000313|EMBL:AJE18252.1,
RC   ECO:0000313|Proteomes:UP000031392};
RX   PubMed=26162030;
RA   Veyrier F.J., Biais N., Morales P., Belkacem N., Guilhen C., Ranjeva S.,
RA   Sismeiro O., Pehau-Arnaudet G., Rocha E.P., Werts C., Taha M.K.,
RA   Boneca I.G.;
RT   "Common Cell Shape Evolution of Two Nasopharyngeal Pathogens.";
RL   PLoS Genet. 11:E1005338-E1005338(2015).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-(5-phospho-beta-D-ribosyl)-5-[(5-phospho-beta-D-
CC         ribosylamino)methylideneamino]imidazole-4-carboxamide = 5-[(5-
CC         phospho-1-deoxy-D-ribulos-1-ylimino)methylamino]-1-(5-phospho-beta-D-
CC         ribosyl)imidazole-4-carboxamide; Xref=Rhea:RHEA:15469,
CC         ChEBI:CHEBI:58435, ChEBI:CHEBI:58525; EC=5.3.1.16;
CC         Evidence={ECO:0000256|ARBA:ARBA00000901, ECO:0000256|HAMAP-
CC         Rule:MF_01014, ECO:0000256|RuleBase:RU003658};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC       from 5-phospho-alpha-D-ribose 1-diphosphate: step 4/9.
CC       {ECO:0000256|ARBA:ARBA00005133, ECO:0000256|HAMAP-Rule:MF_01014,
CC       ECO:0000256|RuleBase:RU003658}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC       ECO:0000256|HAMAP-Rule:MF_01014, ECO:0000256|RuleBase:RU003658}.
CC   -!- SIMILARITY: Belongs to the HisA/HisF family.
CC       {ECO:0000256|ARBA:ARBA00009667, ECO:0000256|HAMAP-Rule:MF_01014,
CC       ECO:0000256|RuleBase:RU003657}.
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DR   EMBL; CP007726; AJE18252.1; -; Genomic_DNA.
DR   EMBL; ADBF01000253; EFE48577.1; -; Genomic_DNA.
DR   RefSeq; WP_003774518.1; NZ_CP007726.1.
DR   AlphaFoldDB; D4DTZ4; -.
DR   STRING; 546263.NELON_04660; -.
DR   KEGG; nel:NELON_04660; -.
DR   PATRIC; fig|546263.7.peg.992; -.
DR   HOGENOM; CLU_048577_1_1_4; -.
DR   UniPathway; UPA00031; UER00009.
DR   Proteomes; UP000005536; Unassembled WGS sequence.
DR   Proteomes; UP000031392; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003949; F:1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide isomerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd04732; HisA; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   HAMAP; MF_01014; HisA; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR006062; His_biosynth.
DR   InterPro; IPR006063; HisA_bact_arch.
DR   InterPro; IPR044524; Isoase_HisA-like.
DR   InterPro; IPR023016; Isoase_HisA-like_bact.
DR   InterPro; IPR011060; RibuloseP-bd_barrel.
DR   NCBIfam; TIGR00007; 1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide isomerase; 1.
DR   PANTHER; PTHR43090; 1-(5-PHOSPHORIBOSYL)-5-[(5-PHOSPHORIBOSYLAMINO)METHYLIDENEAMINO] IMIDAZOLE-4-CARBOXAMIDE ISOMERASE; 1.
DR   PANTHER; PTHR43090:SF2; 1-(5-PHOSPHORIBOSYL)-5-[(5-PHOSPHORIBOSYLAMINO)METHYLIDENEAMINO] IMIDAZOLE-4-CARBOXAMIDE ISOMERASE; 1.
DR   Pfam; PF00977; His_biosynth; 1.
DR   SUPFAM; SSF51366; Ribulose-phoshate binding barrel; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW   Rule:MF_01014};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01014, ECO:0000256|RuleBase:RU003658};
KW   Histidine biosynthesis {ECO:0000256|ARBA:ARBA00023102, ECO:0000256|HAMAP-
KW   Rule:MF_01014};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_01014};
KW   Reference proteome {ECO:0000313|Proteomes:UP000031392}.
FT   ACT_SITE        8
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01014"
FT   ACT_SITE        131
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01014"
SQ   SEQUENCE   246 AA;  25953 MW;  D3FDD11A1A44FE1E CRC64;
     MLLIPAIDLK DGNCVRLRQG LMEDATVFSD QPADMASHWR QQGARRLHLV DLNGAFAGEP
     KNFPAIREIL AAVAADIPVQ LGGGIRDLAT IEKYLTLGLT DVIIGTAAVK NPAFVREACR
     EFAGHIIVGI DAKDGMAAID GWATVTEHRA ADLGRRFADD GVNSIIYTDI GRDGMMSGVN
     IDATVKLAEA VGIPVIASGG LTDLNDIRAL CAAEKDGVTG AITGRAIYEG SIDFAQAQRL
     ADSLGE
//

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