A9G8Y4 (A9G8Y4_SORC5) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Recommended name:
Histidinol-phosphate aminotransferase 3 HAMAP MF_01023
EC=2.6.1.9 HAMAP MF_01023

Alternative name(s):
Imidazole acetol-phosphate transaminase 3 HAMAP MF_01023

Gene names

Name:	hisC4 EMBL CAN99087.1
Synonyms:	hisC3 HAMAP MF_01023
Ordered Locus Names:	sce8915

Organism

Sorangium cellulosum (strain So ce56) (Polyangium cellulosum (strain So ce56)) [Complete proteome] [HAMAP]

Taxonomic identifier

448385 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Deltaproteobacteria › Myxococcales › Sorangiineae › Polyangiaceae › Sorangium

Protein attributes

Sequence length	360 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Catalytic activity	L-histidinol phosphate + 2-oxoglutarate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate. HAMAP MF_01023 SAAS SAAS005861
Cofactor	Pyridoxal phosphate By similarity. HAMAP MF_01023 SAAS SAAS005861
Pathway	Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9. HAMAP MF_01023 SAAS SAAS005861
Subunit structure	Homodimer By similarity. HAMAP MF_01023
Sequence similarities	Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. Histidinol-phosphate aminotransferase subfamily. HAMAP MF_01023

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Histidine biosynthesis HAMAP MF_01023 SAAS SAAS005861
Ligand	Pyridoxal phosphate HAMAP MF_01023 SAAS SAAS005861
Molecular function	Aminotransferase HAMAP MF_01023 SAAS SAAS005861 EMBL CAN99087.1 Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	histidine biosynthetic process Inferred from electronic annotation. Source: HAMAP
Molecular function	1-aminocyclopropane-1-carboxylate synthase activity Inferred from electronic annotation. Source: InterPro L-phenylalanine:2-oxoglutarate aminotransferase activity Inferred from electronic annotation. Source: EC histidinol-phosphate transaminase activity Inferred from electronic annotation. Source: HAMAP pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Amino acid modifications
	Modified residue	224	1	N6-(pyridoxal phosphate)lysine By similarity HAMAP MF_01023

Sequences

	Sequence		Length	Mass (Da)
	A9G8Y4 [UniParc]. Last modified February 5, 2008. Version 1. Checksum: 17F11C8B628ECA1E	FASTA	360	39,275
	10 20 30 40 50 60 MSALVLPSVE LLSPYETGKP LDELARELGV TDAVKLASNE NPLGPSPRAL EAARRALESV 70 80 90 100 110 120 HLYPDGAAYR LRERLAAVHG VTMEEIVQGN GSNELLDLIV HAFATPGSHI VFADPAFVVY 130 140 150 160 170 180 KLAALAYGVP FTAVPLRDLR HDLEAMAAAV TPKTRLLFIA NPNNPTGTHV GRAAVERLLR 190 200 210 220 230 240 ELPPEVIVVM DEAYIQYADA ADFPDSMRLR GLRERLLVLR TFSKIYGLAG FRVGYAVGPV 250 260 270 280 290 300 QLIDYLNRVR APFNVSALAQ AAAVAALDDA EHVEKSRALN LRERDRLTRE LTRLGLSVAP 310 320 330 340 350 360 SQANFVLVDV GRPARPVYDA LLRKGVIVRP FGNLPTSLRV TIGTERENQR FLDSLSAVLA

References

[1]

"Complete genome sequence of the myxobacterium Sorangium cellulosum." Schneiker S., Perlova O., Kaiser O., Gerth K., Alici A., Altmeyer M.O., Bartels D., Bekel T., Beyer S., Bode E., Bode H.B., Bolten C.J., Choudhuri J.V., Doss S., Elnakady Y.A., Frank B., Gaigalat L., Goesmann A. , Groeger C., Gross F., Jelsbak L., Jelsbak L., Kalinowski J., Kegler C., Knauber T., Konietzny S., Kopp M., Krause L., Krug D., Linke B., Mahmud T., Martinez-Arias R., McHardy A.C., Merai M., Meyer F., Mormann S., Munoz-Dorado J., Perez J., Pradella S., Rachid S., Raddatz G., Rosenau F., Rueckert C., Sasse F., Scharfe M., Schuster S.C., Suen G., Treuner-Lange A., Velicer G.J., Vorholter F.-J., Weissman K.J., Welch R.D., Wenzel S.C., Whitworth D.E., Wilhelm S., Wittmann C., Bloecker H., Puehler A., Mueller R. Nat. Biotechnol. 25:1281-1289(2007) [PubMed: 17965706] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	AM746676 Genomic DNA. Translation: CAN99087.1.
RefSeq	YP_001619567.1. NC_010162.1.
3D structure databases
ProteinModelPortal	A9G8Y4.
ModBase	Search...
Protein-protein interaction databases
STRING	A9G8Y4.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	5813060.
GenomeReviews	Gene locus sce8915 in contig AM746676_GR.
KEGG	scl:sce8915.
PATRIC	23677065. VBISorCel80414_9720.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG646350.
OMA	YIELADI.
Family and domain databases
HAMAP	MF_01023. HisC_aminotrans_2. [Tree]
InterPro	IPR001176. ACC_synthase. IPR004839. Aminotransferase_I/II. IPR005861. HisP_aminotrans. IPR015424. PyrdxlP-dep_Trfase_major_dom. IPR015421. PyrdxlP-dep_Trfase_major_sub1. IPR015422. PyrdxlP-dep_Trfase_major_sub2. [Graphical view]
Gene3D	G3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit. G3DSA:3.90.1150.10. PyrdxlP-dep_Trfase_major_sub2. 1 hit.
KO	K00817.
Pfam	PF00155. Aminotran_1_2. 1 hit. [Graphical view]
PRINTS	PR00753. ACCSYNTHASE.
SUPFAM	SSF53383. PyrdxlP-dep_Trfase_major. 1 hit.
TIGRFAMs	TIGR01141. HisC. 1 hit.
ProtoNet	Search...

Entry information

Entry name

A9G8Y4_SORC5

Accession

Primary (citable) accession number: A9G8Y4

Entry history

Integrated into UniProtKB/TrEMBL:	February 5, 2008
Last sequence update:	February 5, 2008
Last modified:	December 14, 2011
This is version 29 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)