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 A9IKD8

Entry ID Method Resolution Chain Position Source
AF-A9IKD8-F1 Predicted AlphaFoldDB

No variants for A9IKD8

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for A9IKD8

No associated diseases with A9IKD8

2 regional properties for A9IKD8

Type Name Position InterPro Accession
domain Cobalamin-independent methionine synthase MetE, C-terminal/archaeal 437 - 759 IPR002629
domain Cobalamin-independent methionine synthase MetE, N-terminal 4 - 319 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
MTITHNLGFP RIGAQRELKR AVEAYWSGKK TAADLEETGR ELRAAHWQRQ AASGLQWVPV
70 80 90 100 110 120
GDFAWYDHIL EWTTLLGAVP ARFGQPEGQP VSLDTLFRMG RGRAPSGTPT AACEMTKWFD
130 140 150 160 170 180
TNYHYIVPEL VPGQTFRIAR EYLFEQVQEA QALGHQVKPV IPGPLTWLWQ GKGDAYAGGA
190 200 210 220 230 240
SDAAKLQLLD TLLPVYAEVL ARLARLGVEW VQIDEPILVL DLPQAWRDAF RTAYARLADA
250 260 270 280 290 300
PVKLLVATYF GGLNDNLATA LALPVAGLHV DLIRAPGQLQ DVAAGLRPGQ VLSAGIIDGR
310 320 330 340 350 360
NIWRTDLDAA LAALAPARQL LGERLWLAPS CSLLHVPVDL ANETDLDAEL RSWLSFAAQK
370 380 390 400 410 420
LDELGLLGRA LADARAPGVD EALAAQRAAL RARRQSARIH NPAVGRRMAE SNAVTRERAP
430 440 450 460 470 480
FAERIARQQQ LLKLPAFPTT TIGSFPQTAE IRALRRDWKS GALSDSAYEA AIRKEIESVI
490 500 510 520 530 540
RFQEKIGLDV LVHGEPERND MVEYFGELLA GFAFTRNGWV QSYGSRCVKP PIIFGDVARP
550 560 570 580 590 600
APMTVGWSSY AQSLTDKPVK GMLTGPVTIL QWSFVRDDQP REQTCRQLAL ALRDEVVDLE
610 620 630 640 650 660
QAGVRVIQID EPAIREGLPL RRADWQAYLD WAVDCFRLST AGVAADTQIH THMCYSEFND
670 680 690 700 710 720
IIESIAAMDA DVITIETSRS NMELLKAFED FRYPNDIGPG VYDIHSPNVP DVDWMVGLMR
730 740 750 760
KAAGRLPSER LWVNPDCGLK TRAWPETEAA LVGMVEAARA LRAG