Q92MG0 (HIS81_RHIME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Histidinol-phosphate aminotransferase 1
EC=2.6.1.9

Alternative name(s):
Imidazole acetol-phosphate transaminase 1

Gene names

Name:	hisC1
Ordered Locus Names:	R02662
ORF Names:	SMc00710

Organism

Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium meliloti) [Complete proteome] [HAMAP]

Taxonomic identifier

266834 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Rhizobiaceae › Sinorhizobium/Ensifer group › Sinorhizobium

Protein attributes

Sequence length	368 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
Cofactor	Pyridoxal phosphate By similarity. HAMAP MF_01023
Pathway	Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9. HAMAP MF_01023
Subunit structure	Homodimer By similarity. HAMAP MF_01023
Sequence similarities	Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. Histidinol-phosphate aminotransferase subfamily.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Histidine biosynthesis
Ligand	Pyridoxal phosphate
Molecular function	Aminotransferase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	histidine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
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: EC 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
Molecule processing
	Chain	1 – 368	368	Histidinol-phosphate aminotransferase 1 HAMAP MF_01023		PRO_0000153435
Amino acid modifications
	Modified residue	224	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q92MG0 [UniParc]. Last modified December 1, 2001. Version 1. Checksum: 3168EF45EF7D8046	FASTA	368	39,171
	10 20 30 40 50 60 MNLALKSPAP RSGILDIAAY VPGKEHAPGV AKVHKLSSNE TPLGASPRAI EAFQKAAFNL 70 80 90 100 110 120 ERYPDGQANA LKEAIAAVHG LNPANILCGN GSDELLGLLC HTYLGPGDEG IVTEHGFLVY 130 140 150 160 170 180 KIQITASGGT PVTVKERQER VDVDAILAAV TERTKIVFIA NPANPTGTYI PVEEVRRLHA 190 200 210 220 230 240 GLPAGVLLVL DAAYAEYVRR NDYEAGLELV SSNRNVVMTR TFSKIYGLAG LRIGWMYAPR 250 260 270 280 290 300 DVVEALDRVR GPFNLNAAAI AAGAAAIRDQ AFVAAAVDQN HTWLAKIGQA LTDIGLRVTP 310 320 330 340 350 360 SVTNFVLIHF PEEAGMSASD ADAYLTSRGF ILRAVGAYGF PNALRMTIGS EEANKGVVAA LTEFMGRK

References

[1]

"Analysis of the chromosome sequence of the legume symbiont Sinorhizobium meliloti strain 1021." Capela D., Barloy-Hubler F., Gouzy J., Bothe G., Ampe F., Batut J., Boistard P., Becker A., Boutry M., Cadieu E., Dreano S., Gloux S., Godrie T., Goffeau A., Kahn D., Kiss E., Lelaure V., Masuy D. , Pohl T., Portetelle D., Puehler A., Purnelle B., Ramsperger U., Renard C., Thebault P., Vandenbol M., Weidner S., Galibert F. Proc. Natl. Acad. Sci. U.S.A. 98:9877-9882(2001) [PubMed: 11481430] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 1021.

[2]

"The composite genome of the legume symbiont Sinorhizobium meliloti." Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F., Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G., Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P., Cowie A. , Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S., Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I., Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S., Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C., Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R., Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H., Wong K., Yeh K.-C., Batut J. Science 293:668-672(2001) [PubMed: 11474104] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 1021.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL591688 Genomic DNA. Translation: CAC47241.1.
RefSeq	NP_386768.1. NC_003047.1.
3D structure databases
ProteinModelPortal	Q92MG0.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1234337.
GenomeReviews	Gene locus R02662 in contig AL591688_GR.
KEGG	sme:SMc00710.
NMPDR	fig|266834.1.peg.3956.
PATRIC	23634861. VBISinMel96828_4162.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG646350.
OMA	GFLVYRI.
ProtClustDB	PRK02731.
Enzyme and pathway databases
BioCyc	SMEL266834:SMC00710-MONOMER.
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.
PROSITE	PS00599. AA_TRANSFER_CLASS_2. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

HIS81_RHIME

Accession

Primary (citable) accession number: Q92MG0

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 11, 2002
Last sequence update:	December 1, 2001
Last modified:	January 25, 2012
This is version 69 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program