Q9X0D0 (HIS8_THEMA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Histidinol-phosphate aminotransferase
EC=2.6.1.9

Alternative name(s):
Imidazole acetol-phosphate transaminase

Gene names

Name:	hisC
Ordered Locus Names:	TM_1040

Organism

Thermotoga maritima

Taxonomic identifier

2336 [NCBI]

Taxonomic lineage

Bacteria › Thermotogae › Thermotogales › Thermotogaceae › Thermotoga

Protein attributes

Sequence length	335 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

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. Ref.2
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	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	histidine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	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 – 335

335

Histidinol-phosphate aminotransferase HAMAP MF_01023

PRO_0000153470

Amino acid modifications

Modified residue

202

1

N6-(pyridoxal phosphate)lysine HAMAP MF_01023

Secondary structure

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335

Helix Strand Turn

Details...

Helix

2 – 5

4

Beta strand

21 – 26

6

Helix

35 – 43

9

Helix

47 – 51

5

Helix

59 – 69

11

Helix

76 – 78

3

Beta strand

79 – 84

6

Helix

85 – 95

11

Beta strand

96 – 101

6

Beta strand

103 – 105

3

Helix

108 – 116

9

Beta strand

119 – 122

4

Beta strand

140 – 147

8

Turn

149 – 151

3

Helix

157 – 165

9

Beta strand

169 – 173

5

Helix

177 – 180

4

Helix

185 – 189

5

Beta strand

192 – 200

9

Turn

201 – 204

4

Helix

207 – 209

3

Beta strand

212 – 216

5

Helix

218 – 227

10

Helix

235 – 246

12

Helix

248 – 272

25

Beta strand

281 – 287

7

Helix

291 – 302

12

Beta strand

305 – 310

6

Beta strand

313 – 317

5

Helix

321 – 332

12

Sequences

	Sequence		Length	Mass (Da)
	Q9X0D0 [UniParc]. Last modified November 1, 1999. Version 1. Checksum: D7CA1B807825376A	FASTA	335	39,298
	10 20 30 40 50 60 MNPLDLIAKR AYPYETEKRD KTYLALNENP FPFPEDLVDE VFRRLNSDAL RIYYDSPDEE 70 80 90 100 110 120 LIEKILSYLD TDFLSKNNVS VGNGADEIIY VMMLMFDRSV FFPPTYSCYR IFAKAVGAKF 130 140 150 160 170 180 LEVPLTKDLR IPEVNVGEGD VVFIPNPNNP TGHVFEREEI ERILKTGAFV ALDEAYYEFH 190 200 210 220 230 240 GESYVDFLKK YENLAVIRTF SKAFSLAAQR VGYVVASEKF IDAYNRVRLP FNVSYVSQMF 250 260 270 280 290 300 AKVALDHREI FEERTKFIVE ERERMKSALR EMGYRITDSR GNFVFVFMEK EEKERLLEHL 310 320 330 RTKNVAVRSF REGVRITIGK REENDMILRE LEVFK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Evidence for lateral gene transfer between Archaea and Bacteria from genome sequence of Thermotoga maritima." Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M., Cotton M.D., Pratt M.S. , Phillips C.A., Richardson D.L., Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M. Nature 399:323-329(1999) [PubMed: 10360571] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.
[2]	"Structural studies of the catalytic reaction pathway of a hyperthermophilic histidinol-phosphate aminotransferase." Fernandez F.J., Vega M.C., Lehmann F., Sandmeier E., Gehring H., Christen P., Wilmanns M. J. Biol. Chem. 279:21478-21488(2004) [PubMed: 15007066] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) OF 6-335, SUBUNIT.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AE000512 Genomic DNA. Translation: AAD36117.1.

PIR

G72304.

RefSeq

NP_228846.1. NC_000853.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1H1C	X-ray	2.85	A/B/C/D	1-335	[»]
1UU0	X-ray	2.85	A/B/C/D	1-335	[»]
1UU1	X-ray	2.38	A/B/C/D	1-335	[»]
1UU2	X-ray	2.80	A/B	1-335	[»]
2F8J	X-ray	2.40	A/B/C/D	1-335	[»]

ProteinModelPortal

Q9X0D0.

SMR

Q9X0D0. Positions 1-335.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

897350.

GenomeReviews

Gene locus TM_1040 in contig AE000512_GR.

KEGG

tma:TM1040.

NMPDR

fig|243274.1.peg.1030.

PATRIC

23937009. VBITheMar51294_1053.

TIGR

TM_1040.

Phylogenomic databases

HOGENOM

HBG646350.

OMA

HANFLLA.

PhylomeDB

Q9X0D0.

ProtClustDB

PRK14808.

Enzyme and pathway databases

BioCyc

TMAR243274:TM_1040-MONOMER.

BRENDA

2.6.1.9. 6331.

Family and domain databases

HAMAP

MF_01023. HisC_aminotrans_2.
[Tree]

InterPro

IPR001917. Aminotrans_II_pyridoxalP_BS.
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]

SUPFAM

SSF53383. PyrdxlP-dep_Trfase_major. 1 hit.

TIGRFAMs

TIGR01141. HisC. 1 hit.

PROSITE

PS00599. AA_TRANSFER_CLASS_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

HIS8_THEMA

Accession

Primary (citable) accession number: Q9X0D0

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 11, 2002
Last sequence update:	November 1, 1999
Last modified:	January 25, 2012
This is version 82 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program