Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

1 structures for Q89AX7

Entry ID Method Resolution Chain Position Source
AF-Q89AX7-F1 Predicted AlphaFoldDB

No variants for Q89AX7

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q89AX7

No associated diseases with Q89AX7

2 regional properties for Q89AX7

Type Name Position InterPro Accession
binding_site Aminotransferase, class-II, pyridoxal-phosphate binding site 208 - 217 IPR001917
domain Aminotransferase, class I/classII 48 - 340 IPR004839

Functions

Description
EC Number 2.6.1.9 Transaminases
Subcellular Localization
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

No GO annotations of cellular component

Name Definition
No GO annotations for cellular component

2 GO annotations of molecular function

Name Definition
histidinol-phosphate transaminase activity Catalysis of the reaction: L-histidinol-phosphate + 2-oxoglutarate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate.
pyridoxal phosphate binding Binding to pyridoxal 5' phosphate, 3-hydroxy-5-(hydroxymethyl)-2-methyl4-pyridine carboxaldehyde 5' phosphate, the biologically active form of vitamin B6.

1 GO annotations of biological process

Name Definition
histidine biosynthetic process The chemical reactions and pathways resulting in the formation of histidine, 2-amino-3-(1H-imidazol-4-yl)propanoic acid.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MDIKKLVRKN ILQLVPYQSA RSIGGNGDVW LNANEFPISS CLSLINISLN RYPEFQPKKL
70 80 90 100 110 120
LNAYAFYLGI CSEKILVTRG SDEAIELLIK TFCEPRKDKI MYFPPTYDMY DISAKILNVE
130 140 150 160 170 180
SIGIPLLKSF QLDLNLIFRN ICGVKLIYLC NPNNPTGNLI KKQDIIALLT YTKGKALIVV
190 200 210 220 230 240
DEAYIEFCAM HSIVQLIEKY SNLVVLRTLS KAFSLAGLRC GFLLSNSNII KMLSKVINPY
250 260 270 280 290 300
PISLPVSDLA TQSLSKKNID IMNSRVLDLN KTRVWFVKQL RTMYCINTIF DSVANYFLVK
310 320 330 340 350
FHDSKLVFKE LWENKVIVRD QNKKTNLKNC IRISVGTRLE CFEVIRILER IDRLYKNVRR