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 A3N1F9

Entry ID Method Resolution Chain Position Source
AF-A3N1F9-F1 Predicted AlphaFoldDB

No variants for A3N1F9

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for A3N1F9

No associated diseases with A3N1F9

2 regional properties for A3N1F9

Type Name Position InterPro Accession
domain Cobalamin-independent methionine synthase MetE, C-terminal/archaeal 427 - 749 IPR002629
domain Cobalamin-independent methionine synthase MetE, N-terminal 5 - 307 IPR013215

Functions

Description
EC Number 2.1.1.14 Methyltransferases
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
5-methyltetrahydropteroyltriglutamate-homocysteine S-methyltransferase activity Catalysis of the reaction: 5-methyltetrahydropteroyltri-L-glutamate + L-homocysteine = L-methionine + tetrahydropteroyltri-L-glutamate.
zinc ion binding Binding to a zinc ion (Zn).

2 GO annotations of biological process

Name Definition
methionine biosynthetic process The chemical reactions and pathways resulting in the formation of methionine (2-amino-4-(methylthio)butanoic acid), a sulfur-containing, essential amino acid found in peptide linkage in proteins.
methylation The process in which a methyl group is covalently attached to a molecule.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MTTLHILGFP RVGAKRELKF AQERYWRKEL AEQDLLDLAK ALREKNWLHQ AQADADFVTV
70 80 90 100 110 120
GDFTFYDHIL DLQVATGAIP ARFGFDSQTL SLDQYFQLAR GNKEQFAIEM TKWFDTNYHY
130 140 150 160 170 180
LVPEFQKNTT FKANPTHYVN QIREAKAAGH QVKPVIVGPL TFLWLGKEKG EAFNRFDLLK
190 200 210 220 230 240
QLVPIYFEIL TALAAEGVEW IQIDEPALAL DLPQEWLAAY QDVYAQLAKV NAKLLLATYF
250 260 270 280 290 300
GSVAEHADLL KALPVDGLHL DLVRAPEQLS AFEDYPKVLS AGVIDGRNIW RANLNRVLDV
310 320 330 340 350 360
LEPLKAKFNQ RLWIAPSCSL LHTPYDLAVE TQLQQNNPEL YRWLAFTLQK VAELQVLKQA
370 380 390 400 410 420
LNAGRDAVTE QLNDSQTAAD ARANSNVIHK AEVAQRLANL PANADKRQSP FAERIKLQNK
430 440 450 460 470 480
WLNLPLLPTT NIGSFPQTLE IRHARAAFKK GELSLADYEA AMKKEIEFVV RKQEELDLDV
490 500 510 520 530 540
LVHGEGERND MVEYFGELLD GFAFTKFGWV QSYGSRCVKP PVIYGDVTRP EPMTVRWSQY
550 560 570 580 590 600
AQSLTDKVMK GMLTGPVTIL QWSFVRNDIP RSTVCKQIGV ALSDEVLDLE KAGIKVIQID
610 620 630 640 650 660
EPAIREGLPL KRADWDAYLQ WAGEAFRLSY MGVKDDTQIH THMCYSEFND ILPAIAGLDA
670 680 690 700 710 720
DVITIETSRS DMELLTAFAD FKYPNDIGPG VYDIHSPRVP TAGEIEHLLR KALKVIPKER
730 740 750
LWVNPDCGLK TRGWKETIEQ LQVMVEVTKK LRAELAE